Any feedback?
No. of entries
Information on EC 3.6.4.B10 - chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)
for references in articles please use BRENDA:EC3.6.4.B10
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Old data from external sources may still be available.
Please check here for current data: EC unknown
Please check here for current data: EC unknown
preliminary BRENDA-supplied EC number
EC Tree 3 Hydrolases
3.6 Acting on acid anhydrides
3.6.4 Acting on acid anhydrides to facilitate cellular and subcellular movement
3.6.4.B10 chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)
The expected taxonomic range for this enzyme is: Archaea, Bacteria, Eukaryota
- 3.6.4.B10
- chaperonins
- tubulins
- actin
-
hetero-oligomeric
- cytoskeletal
- groel
- prefoldin
-
chaperonin-containing
- huntingtin
-
proteostasis
-
double-ring
-
tailless
-
polyglutamine
-
polyq
-
inter-ring
-
phosducin-like
- synthesis
-
back-to-back
- drug development
-
protein-folding
-
homo-oligomeric
- acidophilum
- beta-tubulin
-
thermoplasma
- medicine
-
cryo-electron
showSynonyms
tcp-1, t-complex protein 1, cct complex, tric/cct, chaperonin containing tcp-1, eukaryotic chaperonin, cct/tric, cct chaperonin, chaperonin tric/cct, chaperonin tric, more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CCT
CCT ATPase
CCT chaperonin
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
CCT complex
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
CCT/TRiC
CCT/TRiC chaperonin
chaperonin containing t-complex polypeptide-1
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
-
chaperonin containing TCP-1
chaperonin containing TCP-1 complex
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
chaperonin TCP-1 ring complex
chaperonin TRiC
chaperonin TRiC/CCT
chaperonin-containing t-complex polypeptide 1
chaperonin-containing TCP-1 complex
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
CpkB
cytosolic chaperonin
cytosolic chaperonin containing TCP-1
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
eukaryotic chaperonin
eukaryotic chaperonin TRiC
eukaryotic group II chaperonin
GaTRiC
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
-
group II chaperonin
LdTCP1
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
LdTCP1epsilon
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
subunit
PfTRiC
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
PhCPN
Plasmodium TRiC
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
ring complex TRiC
ring-shaped chaperonin TCP-1 ring complex
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
T-complex polypeptide-1 ring complex
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
-
T-complex protein 1
T-complex protein 1 ring complex
T-complex protein 1 subunit epsilon
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
UniProt
T-complex protein-1
T-complex protein-1 ring complex
Tailless complex polypeptide 1
tailless complex polypeptide I ring complex
F6T521; F6PJP5; G7MDZ6; A0A5F7ZBU8; A0A1D5Q8I4; I0FKJ8; A0A1D5RDC8; A0A5F7Z7P5
-
TCP-1
TCP-1 ring complex
thermosome
TKS1-CPN
TriC
TRiC chaperonin
TRiC/CCT
TRiC/CCT chaperonin
type II chaperonin
CCT
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
-
CCT
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
CCT
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
-
CCT
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
-
CCT
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
CCT
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
CCT
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
-
-
CCT ATPase
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
-
CCT ATPase
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
-
CCT ATPase
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
-
-
CCT ATPase
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
-
CCT ATPase
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
CCT ATPase
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
CCT ATPase
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
-
CCT ATPase
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
-
-
CCT/TRiC
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
-
CCT/TRiC
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
-
CCT/TRiC
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
-
-
CCT/TRiC
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
-
CCT/TRiC
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
CCT/TRiC
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
CCT/TRiC
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
-
-
chaperonin containing TCP-1
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
chaperonin containing TCP-1
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
chaperonin containing TCP-1
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
-
chaperonin containing TCP-1
Leishmania donovani MHOM/IN/80
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
-
chaperonin TCP-1 ring complex
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
chaperonin TCP-1 ring complex
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
-
chaperonin TRiC
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
chaperonin TRiC
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
-
chaperonin TRiC
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
chaperonin TRiC/CCT
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
-
chaperonin-containing t-complex polypeptide 1
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
-
chaperonin-containing t-complex polypeptide 1
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
-
-
eukaryotic chaperonin
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
-
eukaryotic chaperonin
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
-
eukaryotic chaperonin
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
-
eukaryotic chaperonin
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
-
-
eukaryotic chaperonin
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
-
eukaryotic chaperonin
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
-
eukaryotic chaperonin
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
eukaryotic chaperonin
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
-
eukaryotic chaperonin
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
eukaryotic chaperonin
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
-
eukaryotic chaperonin
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
-
-
group II chaperonin
Pyrococcus species contain only one chaperonin gene per whole genome
group II chaperonin
Pyrococcus species contain only one chaperonin gene per whole genome
-
PhCPN
Pyrococcus species contain only one chaperonin gene per whole genome
PhCPN
Pyrococcus species contain only one chaperonin gene per whole genome
-
T-complex protein 1
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
T-complex protein 1
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
-
T-complex protein 1
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
T-complex protein 1 ring complex
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
T-complex protein-1
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
T-complex protein-1
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
-
T-complex protein-1
Leishmania donovani MHOM/IN/80
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
-
T-complex protein-1 ring complex
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
T-complex protein-1 ring complex
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
-
T-complex protein-1 ring complex
Leishmania donovani MHOM/IN/80
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
-
TCP-1
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
-
TCP-1
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
-
TCP-1
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
TCP-1
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
TCP-1
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
-
TCP-1
Leishmania donovani MHOM/IN/80
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
-
TCP-1
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
TCP-1
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
-
-
TCP-1 ring complex
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
TriC
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
TriC
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
-
TriC
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
-
TriC
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
TriC
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
-
TriC
Leishmania donovani MHOM/IN/80
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
-
-
TriC
F6T521; F6PJP5; G7MDZ6; A0A5F7ZBU8; A0A1D5Q8I4; I0FKJ8; A0A1D5RDC8; A0A5F7Z7P5
-
TriC
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
TriC
-
-
TRiC chaperonin
F6T521; F6PJP5; G7MDZ6; A0A5F7ZBU8; A0A1D5Q8I4; I0FKJ8; A0A1D5RDC8; A0A5F7Z7P5
-
TRiC/CCT
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
TRiC/CCT chaperonin
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ATP + H2O = ADP + phosphate
enzymes exists as a homooligomer in a double-ring structure, which captures non-native proteins in a central cavity to promote correct folding in an ATP-dependent manner
ATP + H2O = ADP + phosphate
formation of prefoldin-bound alph- and beta-tubulin complexes. TRiC addition to prefoldin:alpha-tubulin or prefoldin:beta-tubulin complexes leads to formation of a ternary complex with TRiC. ATP addition leads to production of folded protease-resistant tubulin monomer, TRiC promotes ATP-dependent tubulin folding
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
ATP + H2O = ADP + phosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
Substrates: addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: the enzyme protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively, and malate dehydrogenase from thermal inactivation at 80°C and 85°C. In the presence of ATP, the protective effects of alpha- and beta-subunits on citrate synthase from thermal aggregation and inactivation, and alcohol dehydrogenase from thermal aggregation, are more enhanced, whereas cooperation between chaperonins and ATP in protection activity on alcohol dehydrogenase and malate dehydrogenase (at 85°C) from thermal inactivation is not observed. Specifically, the presence of both alpha- and beta- subunits can effectively protect malate dehydrogenase from thermal inactivation at 80°C in an ATP-dependent manner
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: the enzyme protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively, and malate dehydrogenase from thermal inactivation at 80°C and 85°C. In the presence of ATP, the protective effects of alpha- and beta-subunits on citrate synthase from thermal aggregation and inactivation, and alcohol dehydrogenase from thermal aggregation, are more enhanced, whereas cooperation between chaperonins and ATP in protection activity on alcohol dehydrogenase and malate dehydrogenase (at 85°C) from thermal inactivation is not observed. Specifically, the presence of both alpha- and beta- subunits can effectively protect malate dehydrogenase from thermal inactivation at 80°C in an ATP-dependent manner
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: in the presence of ATP, ApCpnB effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Specifically, the activity of malate dehydrogenase (MDH) at 85°C is greatly stabilized by the addition of ApCpnB and ATP
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: enzyme conformational changes upon ATP binding and throughout the ATPase cycle, structure-function relationship, overview
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: the enzyme can protect halophilic proteins against denaturation under conditions of cellular hyposaline stress
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: P45 forms complexes with halophilic malate dehydrogenase during its salt-dependent denaturation/renaturation and decreases the rate of deactivation of the enzyme in an ATP-dependent manner
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: ATP hydrolysis drives the structural change of the TRiC complex
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: enzyme substrates are known to release from CCT in an ATP-dependent manner
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
Leishmania donovani MHOM/IN/80
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
F6T521; F6PJP5; G7MDZ6; A0A5F7ZBU8; A0A1D5Q8I4; I0FKJ8; A0A1D5RDC8; A0A5F7Z7P5
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
-
Substrates: nucleotide binding structure and conformational changes, overview
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
Substrates: the enzyme exists as a homooligomer in a double-ring structure, which captures non-native proteins in a central cavity to promote correct folding in an ATP-dependent manner. It protects the citrate synthase of a porcine heart from thermal aggregation at 45°C, and does the same on the isopropylmalate dehydrogenase of Thermus thermophilus HB8, at 90°C. It enhances the refolding of green fluorescent protein, which has been unfolded by low pH, in an ATP-dependent manner. It is not effective in the refolding of isopropylmalate dehydrogenase, the refolding efficiency is enhanced by the cooperation of the enzyme with Pyrococcus prefoldin
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: activity of the enzyme as a molecular chaperone is examined using hyperthermophilic inorganic phosphatase from Pyrococcus horikoshii as a model substrate. The enzyme protected the inorganic phosphatase from thermal inactivation at 85°C and 110°C
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: the enzyme exists as a homooligomer in a double-ring structure, which captures non-native proteins in a central cavity to promote correct folding in an ATP-dependent manner. It protects the citrate synthase of a porcine heart from thermal aggregation at 45°C, and does the same on the isopropylmalate dehydrogenase of Thermus thermophilus HB8, at 90°C. It enhances the refolding of green fluorescent protein, which has been unfolded by low pH, in an ATP-dependent manner. It is not effective in the refolding of isopropylmalate dehydrogenase, the refolding efficiency is enhanced by the cooperation of the enzyme with Pyrococcus prefoldin
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: nucleotide binding structure and conformational changes, overview
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: ATP hydrolysis drives the structural change of the TRiC complex
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: ATP hydrolysis drives the structural change of the TRiC complex
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
Substrates: the enzyme prevents thermal denaturation and enhances thermostability of Saccharomyces cerevisiae alcohol dehydrogenase. CpkB requires ATP for its chaperonin function at a low CpkB concentration. CpkB functions without ATP when present in excess. CpkB is useful for solubilizing insoluble proteins in vivo
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: nucleotide binding structure and conformational changes, overview
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
CTP + H2O
CDP + phosphate
Substrates: addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP
Products: -
Products: -
?
CTP + H2O
CDP + phosphate
Substrates: -
Products: -
Products: -
?
CTP + H2O
CDP + phosphate
Substrates: addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP
Products: -
Products: -
?
GTP + H2O
GDP + phosphate
Substrates: addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP
Products: -
Products: -
?
GTP + H2O
GDP + phosphate
Substrates: -
Products: -
Products: -
?
GTP + H2O
GDP + phosphate
Substrates: addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP
Products: -
Products: -
?
UTP + H2O
UDP + phosphate
Substrates: addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP
Products: -
Products: -
?
UTP + H2O
UDP + phosphate
Substrates: -
Products: -
Products: -
?
UTP + H2O
UDP + phosphate
Substrates: addition of ApCpnA (subunit alpha) and ApCpnB (subunit beta) effectively protects citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. Purified enzyme hydrolyzes the nucleotides with the following efficacy (from highest to lowest): ATP > CTP > UTP > GTP
Products: -
Products: -
?
additional information
?
-
Substrates: subunits ApCpnA and ApCpnB are able to hydrolyze not only ATP, but also CTP, GTP, and UTP, albeit with different efficacies. Addition of subunits ApCpnA and ApCpnB effectively protects porcine heart citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. In particular, the addition of ATP or CTP to subunits ApCpnA and ApCpnB results in the most effective prevention of thermal aggregation and inactivation of the substrate proteins
Products: -
Products: -
?
additional information
?
-
Substrates: subunits ApCpnA and ApCpnB are able to hydrolyze not only ATP, but also CTP, GTP, and UTP, albeit with different efficacies. Addition of subunits ApCpnA and ApCpnB effectively protects porcine heart citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. In particular, the addition of ATP or CTP to subunits ApCpnA and ApCpnB results in the most effective prevention of thermal aggregation and inactivation of the substrate proteins
Products: -
Products: -
?
additional information
?
-
Substrates: subunits ApCpnA and ApCpnB are able to hydrolyze not only ATP, but also CTP, GTP, and UTP, albeit with different efficacies. Addition of subunits ApCpnA and ApCpnB effectively protects porcine heart citrate synthase and alcohol dehydrogenase from thermal aggregation and inactivation at 43°C and 50°C, respectively. In particular, the addition of ATP or CTP to subunits ApCpnA and ApCpnB results in the most effective prevention of thermal aggregation and inactivation of the substrate proteins
Products: -
Products: -
?
additional information
?
-
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
Substrates: chaperonin TRiC/CCT modulates the folding and activity of leukemogenic fusion oncoprotein AML1-ETO.A folding intermediate of AML1-ETO binds to TRiC directly, mainly through its beta-strand rich, DNA-binding domain (AML-(1-175)), with the assistance of HSP70. TRiC contributes to AML1-ETO proteostasis through specific interactions between the oncoprotein's DNA-binding domain
Products: -
Products: -
?
additional information
?
-
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
Substrates: comparison of the mechanisms of action of the GroEL/GroES and the TRiC chaperonin systems on MreB client protein variants extracted from E.scherichia coli. MreB is a homologue to actin in prokaryotes. Single-molecule fluorescence correlation spectroscopy (FCS) and time-resolved fluorescence polarization anisotropy report the binding interaction of folding MreB with GroEL, GroES and TRiC. Fluorescence resonance energy transfer (FRET) measurements on MreB variants quantifiy molecular distance changes occurring during conformational rearrangements within folding MreB bound to chaperonins
Products: -
Products: -
?
additional information
?
-
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
Substrates: the CCT complex physically interacts with TOR signaling components including TOR, Rheb, and S6K
Products: -
Products: -
?
additional information
?
-
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
Substrates: GaTRiC acts a chaperonin mediating folding of denatured luciferase to the functional stage
Products: -
Products: -
?
additional information
?
-
-
Substrates: GaTRiC acts a chaperonin mediating folding of denatured luciferase to the functional stage
Products: -
Products: -
?
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: TRiC binds to and modulates cancer related proteins
Products: -
Products: -
?
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: chaperonin TRiC/CCT modulates the folding and activity of leukemogenic fusion oncoprotein AML1-ETO.A folding intermediate of AML1-ETO binds to TRiC directly, mainly through its beta-strand rich, DNA-binding domain (AML-(1-175)), with the assistance of HSP70. TRiC contributes to AML1-ETO proteostasis through specific interactions between the oncoprotein's DNA-binding domain. The interaction between AML1-ETO and TRiC is transient. HSP70 facilitates the direct association of AML1-ETO with TRiC
Products: -
Products: -
?
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: reovirus sigma3 is a TRiC substrate
Products: -
Products: -
?
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: chaperonin TRiC/CCT recognizes fusion oncoprotein AML1-ETO through subunit-specific interactions. A folding intermediate of AML1-ETO's DNA-binding domain (AML1-175) forms a stable complex with apo-TRiC. TRiC can refold denatured AML1-175 (DBD) and restore its DNA binding activity in vitro. AML1-175 localizes to specific TRiC subunits, it binds to the apical domains of subunits CCT6 and 8
Products: -
Products: -
?
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: functional cooperation of TRiC and PFD in actin folding. In the absence of PFD, TRiC mediates actin folding with biphasic kinetics. Upon ATP addition, a burst of folding activity (about 4 min) is followed by a much slower and inefficient folding phase that extended up to 60 min. Following ATP addition, PFD enhances the yield of actin folding and disfavored actin aggregation. Substrate folding and PFD interactions, detailed overview. PFD is not merely capturing actin that is released from TRiC due to ATP cycling. Instead, it appears that transfer is mediated by a ternary TRiC-actin-PFD complex, from which actin partitions between TRiC and PFD. Dynamic TRiC-PFD interaction
Products: -
Products: -
?
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: the hetero-oligomeric chaperonin of eukarya, TRiC, is required to fold the cytoskeletal protein actin. Actin fails to fold spontaneously even in the absence of aggregation but populates a kinetically trapped, conformationally dynamic state. Analysis of the unique features of TRiC directing the folding pathway of an obligate eukaryotic substrate, overview. Binding to TRiC stabilizes a native-like structure in actin. ATP binding induces an asymmetric TRiC intermediate and selective actin release. Substrate recognition mechanism by GroEL and TRiC, and folding mechanism of actin overview
Products: -
Products: -
?
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: the nucleoprotein of the mammarenavirus lymphocytic choriomeningitis virus (LCMV) is a substrate of the human TRiC/CCT complex
Products: -
Products: -
-
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: CCT folds a wide range of specific, yet diverse substrates ranging from actin and tubulin, to the beta subunits of G protein heterotrimers (Gbeta) and the 150 kDa RAPTOR subunit of the mammalian target of rapamycin
Products: -
Products: -
-
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: prefoldin-TRiC mediates the folding pathway of the archetype TRiC obligate substrates alpha and beta-tubulin
Products: -
Products: -
-
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: chaperonin protein substrate recognition and binding, folding mechanism, overview. Substrate folding by CCT is a very complex process with the chaperonin actively directing the folding pathway. Both actin and tubulin make specific contacts with CCT upon binding inside the closed chamber, which make use of the inherent asymmetry in the closed ring and available binding surfaces to ensure their domains are folded in the proper order. Tubulin is contacting CCT 6, 8, and 1 and actin is extended with one domain binding CCT 3 and 6 and another binding CCT 2, 7, and 8
Products: -
Products: -
-
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: reconstitution of the folding of beta-tubulin using human prefoldin and TRiC reveals that unstructured beta-tubulin is delivered by prefoldin to the open TRiC chamber followed by ATP-dependent chamber closure. Progressively folded beta-tubulin intermediates form within the closed TRiC chamber, culminating in native tubulin. This substrate folding pathway appears closely guided by site-specific interactions with conserved regions in the TRiC chamber. Initial electrostatic interactions between the TRiC interior wall and both the folded tubulin N-domain and its C-terminal E-hook tail establish the native substrate topology, thus enabling C-domain folding. Intrinsically disordered CCT C-termini within the chamber promote subsequent folding of tubulin's core and middle domains and GTP-binding. Thus, TRiC's chamber provides chemical and topological directives that shape the folding landscape of its obligate substrates. TRiC dependence of beta-tubulin folding, interaction analysis detailed overview
Products: -
Products: -
-
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: the molecular chaperone TRiC/CCT is a DTC1-interacting protein. WDTC1 binds TRiC/CCT through its ADP domain, and TRiC/CCT recognizes and binds WDTC1 through the CCT5 subunit
Products: -
Products: -
-
additional information
?
-
-
Substrates: rhodanese is used as a substrate in the folding assay
Products: -
Products: -
-
additional information
?
-
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
Substrates: the molecular chaperone TRiC/CCT is a DTC1-interacting protein. WDTC1 binds TRiC/CCT through its ADP domain, and TRiC/CCT recognizes and binds WDTC1 through the CCT5 subunit
Products: -
Products: -
-
additional information
?
-
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
Substrates: interactome of the eukaryotic chaperonin CCT and its primary clients, the ubiquitous cytoskeletal proteins, actin and tubulin. 5 Plasmodium specific antigen proteins are detected bound to PfCCT: erythrocyte surface antigen, 101 kDa malarial antigen, liver stage antigen, antigen 332, and ring exported protein
Products: -
Products: -
-
additional information
?
-
-
Substrates: group II chaperonin CPN accomplishes the precise folding of Pyrococcus furiosus citrate synthase and Aequorea enhanced green fluorescence protein in an ATP-dependent manner. Both prefoldin and chaperonin CPN interact with Pyrococcus furiosus citrate synthase and Aequorea enhanced green fluorescence protein refolding intermediates. Effects on the refolding reaction vary from passive effects such as ATP-dependent binding and release of CPN towards GFP protein and binding which leads to folding arrest, prefoldin towards GFP protein, to active effects such as net increase in thermal stability, CPN towards citrate synthase to an active improvement in refolding yield, prefoldin towards citrate synthase. PfuCPN cannot assist the refolding of Pyrococcus furiosus citrate synthase, but may contribute to maintaining its active form, while prefolding facilitates the refolding of Pyrococcus furiosus citrate synthase
Products: -
Products: -
?
additional information
?
-
Substrates: TRiC mediates protein folding by encapsulation. It utilizes a built-in lid mechanism of helical protrusions extending from the apical domains that function similar to the blades of a camera iris. This mechanism allows linker sequences between sequential protein domains to protrude through the narrow oculus of the aperture for domain-wise protein encapsulation. The apical domains of the paralogous subunits differ in their specificity for substrate protein binding, allowing TRiC to mediate the folding of a range of structurally diverse proteins including tubulins and actin, as well as many proteins with WD40 beta-propeller domains. Cavity closure is triggered by ATP hydrolysis, not ATP binding. TRiC also binds and masks polyQ-expanded fragments of the Huntington's disease protein, inhibiting their toxic aggregation
Products: -
Products: -
?
additional information
?
-
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: CCT/TRiC is mixed rapidly with different concentrations of ATP, and the amount of phosphate formed upon ATP hydrolysis is measured as a function of time using the coumarin-labeled phosphate-binding protein method. Two burst phases are observed, followed by a lag phase and then a linear steady-state phase of ATP hydrolysis
Products: -
Products: -
?
additional information
?
-
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: eukaryotic chaperonin TRiC (CCT) shows a staggered ATP binding mechanism, staggrered binding of ATP on the CCT6 side of nucleotide partially preloaded (NPP) stated TRiC. ATP binding affects TRiC inter- and intraring interactions. The ATP binding affinity varies among the eight distinct subunits of TRiC. Multiple modes of nucleotide binding in yeast TRiC, detailed overview. The staggered ATP binding mechanism may actually result from the delayed release of the residual ADP of these three subunits CCT8, CCT6, and CCT3
Products: -
Products: -
?
additional information
?
-
-
Substrates: eukaryotic chaperonin TRiC (CCT) shows a staggered ATP binding mechanism, staggrered binding of ATP on the CCT6 side of nucleotide partially preloaded (NPP) stated TRiC. ATP binding affects TRiC inter- and intraring interactions. The ATP binding affinity varies among the eight distinct subunits of TRiC. Multiple modes of nucleotide binding in yeast TRiC, detailed overview. The staggered ATP binding mechanism may actually result from the delayed release of the residual ADP of these three subunits CCT8, CCT6, and CCT3
Products: -
Products: -
?
additional information
?
-
Substrates: TRiC mediates protein folding by encapsulation. It utilizes a built-in lid mechanism of helical protrusions extending from the apical domains that function similar to the blades of a camera iris. This mechanism allows linker sequences between sequential protein domains to protrude through the narrow oculus of the aperture for domain-wise protein encapsulation. The apical domains of the paralogous subunits differ in their specificity for substrate protein binding, allowing TRiC to mediate the folding of a range of structurally diverse proteins including tubulins and actin, as well as many proteins with WD40 beta-propeller domains. Cavity closure is triggered by ATP hydrolysis, not ATP binding. TRiC also binds and masks polyQ-expanded fragments of the Huntington's disease protein, inhibiting their toxic aggregation
Products: -
Products: -
?
additional information
?
-
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: CCT/TRiC is mixed rapidly with different concentrations of ATP, and the amount of phosphate formed upon ATP hydrolysis is measured as a function of time using the coumarin-labeled phosphate-binding protein method. Two burst phases are observed, followed by a lag phase and then a linear steady-state phase of ATP hydrolysis
Products: -
Products: -
?
additional information
?
-
-
Substrates: ATP-dependent conformational change starts with the high-affinity hemisphere and progresses to the low-affinity hemisphere of the enzyme complex. CtCCT is immobilized on a Strep-Tactin column and acid-denatured actin and tubulin are applied to it. CtCCT is eluted by D-desthiobiotin, CtCCT binds to denatured actin and tubulin. Detailed analysis of ATP-induced conformational change in recombinant CCT using diffracted X-ray tracking, overview
Products: -
Products: -
?
additional information
?
-
Substrates: indole-3-glycerol-phosphate synthase, TrpC, is a specific target protein of CpkA
Products: -
Products: -
?
additional information
?
-
Substrates: indole-3-glycerol-phosphate synthase, TrpC, is a specific target protein of CpkA
Products: -
Products: -
?
additional information
?
-
Substrates: indole-3-glycerol-phosphate synthase, TrpC, is no target protein for CpkB
Products: -
Products: -
?
additional information
?
-
Substrates: indole-3-glycerol-phosphate synthase, TrpC, is no target protein for CpkB
Products: -
Products: -
?
additional information
?
-
Substrates: denatured indole-3-glycerol-phosphate synthase of Thermococcus kodakarensis is a CpkA target in vitro, mutant CpkA-E530G is more effective than wild-type enzyme CpkA at facilitating the refolding of chemically unfolded substrate
Products: -
Products: -
?
additional information
?
-
Substrates: denatured indole-3-glycerol-phosphate synthase of Thermococcus kodakarensis is a CpkA target in vitro, mutant CpkA-E530G is more effective than wild-type enzyme CpkA at facilitating the refolding of chemically unfolded substrate
Products: -
Products: -
?
additional information
?
-
Substrates: ATP-dependent rotational motion of a group II chaperonin
Products: -
Products: -
?
additional information
?
-
Substrates: ATP-dependent rotational motion of a group II chaperonin
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme TKS1-CPN shows a strong protein-folding activity
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme TKS1-CPN shows a strong protein-folding activity
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme assists in folding of IPMDH
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme TKS1-CPN shows a strong protein-folding activity
Products: -
Products: -
?
additional information
?
-
Substrates: ATP-dependent rotational motion of a group II chaperonin
Products: -
Products: -
?
additional information
?
-
Substrates: ATP-dependent rotational motion of a group II chaperonin
Products: -
Products: -
?
additional information
?
-
Substrates: enzyme TKS1-CPN shows a strong protein-folding activity
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
-
Substrates: the enzyme can protect halophilic proteins against denaturation under conditions of cellular hyposaline stress
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
Leishmania donovani MHOM/IN/80
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
F6T521; F6PJP5; G7MDZ6; A0A5F7ZBU8; A0A1D5Q8I4; I0FKJ8; A0A1D5RDC8; A0A5F7Z7P5
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
Substrates: -
Products: -
Products: -
ir
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
ATP + H2O
ADP + phosphate
Substrates: -
Products: -
Products: -
?
additional information
?
-
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
Substrates: chaperonin TRiC/CCT modulates the folding and activity of leukemogenic fusion oncoprotein AML1-ETO.A folding intermediate of AML1-ETO binds to TRiC directly, mainly through its beta-strand rich, DNA-binding domain (AML-(1-175)), with the assistance of HSP70. TRiC contributes to AML1-ETO proteostasis through specific interactions between the oncoprotein's DNA-binding domain
Products: -
Products: -
?
additional information
?
-
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
Substrates: the CCT complex physically interacts with TOR signaling components including TOR, Rheb, and S6K
Products: -
Products: -
?
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: TRiC binds to and modulates cancer related proteins
Products: -
Products: -
?
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: chaperonin TRiC/CCT modulates the folding and activity of leukemogenic fusion oncoprotein AML1-ETO.A folding intermediate of AML1-ETO binds to TRiC directly, mainly through its beta-strand rich, DNA-binding domain (AML-(1-175)), with the assistance of HSP70. TRiC contributes to AML1-ETO proteostasis through specific interactions between the oncoprotein's DNA-binding domain. The interaction between AML1-ETO and TRiC is transient. HSP70 facilitates the direct association of AML1-ETO with TRiC
Products: -
Products: -
?
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: the nucleoprotein of the mammarenavirus lymphocytic choriomeningitis virus (LCMV) is a substrate of the human TRiC/CCT complex
Products: -
Products: -
-
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: CCT folds a wide range of specific, yet diverse substrates ranging from actin and tubulin, to the beta subunits of G protein heterotrimers (Gbeta) and the 150 kDa RAPTOR subunit of the mammalian target of rapamycin
Products: -
Products: -
-
additional information
?
-
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Substrates: prefoldin-TRiC mediates the folding pathway of the archetype TRiC obligate substrates alpha and beta-tubulin
Products: -
Products: -
-
additional information
?
-
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
Substrates: interactome of the eukaryotic chaperonin CCT and its primary clients, the ubiquitous cytoskeletal proteins, actin and tubulin. 5 Plasmodium specific antigen proteins are detected bound to PfCCT: erythrocyte surface antigen, 101 kDa malarial antigen, liver stage antigen, antigen 332, and ring exported protein
Products: -
Products: -
-
additional information
?
-
Substrates: TRiC mediates protein folding by encapsulation. It utilizes a built-in lid mechanism of helical protrusions extending from the apical domains that function similar to the blades of a camera iris. This mechanism allows linker sequences between sequential protein domains to protrude through the narrow oculus of the aperture for domain-wise protein encapsulation. The apical domains of the paralogous subunits differ in their specificity for substrate protein binding, allowing TRiC to mediate the folding of a range of structurally diverse proteins including tubulins and actin, as well as many proteins with WD40 beta-propeller domains. Cavity closure is triggered by ATP hydrolysis, not ATP binding. TRiC also binds and masks polyQ-expanded fragments of the Huntington's disease protein, inhibiting their toxic aggregation
Products: -
Products: -
?
additional information
?
-
Substrates: TRiC mediates protein folding by encapsulation. It utilizes a built-in lid mechanism of helical protrusions extending from the apical domains that function similar to the blades of a camera iris. This mechanism allows linker sequences between sequential protein domains to protrude through the narrow oculus of the aperture for domain-wise protein encapsulation. The apical domains of the paralogous subunits differ in their specificity for substrate protein binding, allowing TRiC to mediate the folding of a range of structurally diverse proteins including tubulins and actin, as well as many proteins with WD40 beta-propeller domains. Cavity closure is triggered by ATP hydrolysis, not ATP binding. TRiC also binds and masks polyQ-expanded fragments of the Huntington's disease protein, inhibiting their toxic aggregation
Products: -
Products: -
?
additional information
?
-
Substrates: indole-3-glycerol-phosphate synthase, TrpC, is a specific target protein of CpkA
Products: -
Products: -
?
additional information
?
-
Substrates: indole-3-glycerol-phosphate synthase, TrpC, is a specific target protein of CpkA
Products: -
Products: -
?
additional information
?
-
Substrates: indole-3-glycerol-phosphate synthase, TrpC, is no target protein for CpkB
Products: -
Products: -
?
additional information
?
-
Substrates: indole-3-glycerol-phosphate synthase, TrpC, is no target protein for CpkB
Products: -
Products: -
?
additional information
?
-
Substrates: denatured indole-3-glycerol-phosphate synthase of Thermococcus kodakarensis is a CpkA target in vitro, mutant CpkA-E530G is more effective than wild-type enzyme CpkA at facilitating the refolding of chemically unfolded substrate
Products: -
Products: -
?
additional information
?
-
Substrates: denatured indole-3-glycerol-phosphate synthase of Thermococcus kodakarensis is a CpkA target in vitro, mutant CpkA-E530G is more effective than wild-type enzyme CpkA at facilitating the refolding of chemically unfolded substrate
Products: -
Products: -
?
additional information
?
-
Substrates: ATP-dependent rotational motion of a group II chaperonin
Products: -
Products: -
?
additional information
?
-
Substrates: ATP-dependent rotational motion of a group II chaperonin
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme assists in folding of IPMDH
Products: -
Products: -
?
additional information
?
-
Substrates: ATP-dependent rotational motion of a group II chaperonin
Products: -
Products: -
?
additional information
?
-
Substrates: ATP-dependent rotational motion of a group II chaperonin
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
phosducin I
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
-
-
phosducin II
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
-
-
phosducin III
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
-
-
phosducin III
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
-
-
phosducin-like cofactor protein
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
three different phosducin-like cofactor proteins
-
phosducin-like cofactor protein
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
PhLP, TRiC subunits and co-chaperones such as prefoldin and phosducin-like proteins interact with the substrate to assist the overall folding process in a substrate-specific manner. PhLP2A binds to the open TRiC chamber and modulates TRiC-PFD interactions. ATP-induced TRiC closure folds the substrate in collaboration with PhLP2A. PhLP2A has bifunctional modules and works as a chaperone-in-chaperonin during the folding cycle
-
phosducin-like cofactor protein
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
PhLP, TRiC subunits and co-chaperones such as prefoldin and phosducin-like proteins interact with the substrate to assist the overall folding process in a substrate-specific manner. PhLP2A binds to the open TRiC chamber and modulates TRiC-PFD interactions. ATP-induced TRiC closure folds the substrate in collaboration with PhLP2A. PhLP2A has bifunctional modules and works as a chaperone-in-chaperonin during the folding cycle
-
phosducin-like cofactor protein
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
cochaperone PhLP2A, PhPL2A binds to the open conformation of the TRiC complex for phosducin-like PhLP2A-chaperonin TRiC cooperation during the ATP-driven folding cycle, ATP-driven PhLP2A structural rearrangement cycle occurs within the TRiC chamber to facilitate folding, structure-function mechanism, detailed overview
-
phosducin-like cofactor protein
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
PhLP1 is involved in folding of the beta-propeller domains of G protein beta subunits. PhLP1 forms a ternary complex with CCT and Gbeta1 that is essential for Gbeta1 folding
-
phosducin-like cofactor protein
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
PhLP2A is a ternary complex between human actin, CCT, and PhLP2A. PhLP2A might act as an anchor to hold actin inside CCT upon ring opening to prevent premature release, which actin is prone to do, thereby slowing the rates of both actin release and ATP hydrolysis while simultaneously promoting proper actin folding
-
phosducin-like cofactor protein
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
PhLP3 promotes beta-tubulin folding
-
phosducin-like cofactor protein
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
PhLP4
-
phosducin-like cofactor protein
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
PhLP1 is involved in folding of the beta-propeller domains of G protein beta subunits. PhLP1 forms a ternary complex with CCT and Gbeta1 that is essential for Gbeta1 folding
-
phosducin-like cofactor protein
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
PhLP2 is an essential gene in yeast. PhLP2 is a CCT co-chaperone in actin and tubulin folding. Co-chaperone role for PhLP2 in CCT-dependent folding of regulators of the G1 to S phase transition in the cell cycle
-
phosducin-like cofactor protein
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
PhLP3 inhibits actin folding in yeast. PhLP3 may also contribute to cytoskeletal function as a CCT co-chaperone, but in a different manner than PhLP2. Genetic deletion of PhLP3 in yeast is not lethal, and PhLP3 overexpression does not rescue PhLP2 deletion
-
phosducin-like cofactor protein
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
PhLPs, are thioredoxin-fold, cofactors which enhance the binding of the actin, tubulin, and Gbeta protein substrates to CCT
-
prefoldin
PFD, is a jellyfish-like hexameric protein that is exclusively found in archaea and eukaryotes, ans is a molecular chaperone that captures an unfolded protein substrate and transfers it to a group II chaperonin (CPN). The transfer of a substrate from PFD to CPN involves a direct interaction, PFD interacts with the apical domain of CPN. Analysis of protein-folding mechanism of PFD and CPN using the PFD-CPN systems of the hyperthermophilic archaea, the C-terminal region contributes to the functional cooperation between PFDalpha1beta1 and CPNbeta, overview. The C-terminus of the PFD alpha subunit is not important for the interaction with CPN and substrate transfer
-
prefoldin
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
PFD, is required for protein substrate folding, PFD pivots around a conserved electrostatic interface with TRiC/CCT, PFD acts on TRiC/CCT-substrate complex to enhance the rate of the folding reaction. PFD alternates between an open latched conformation and a closed engaged conformation that aligns the PFD-TRiC substrate binding chambers. PFD can act after TRiC binds its substrates to enhance the rate and yield of the folding reaction, suppressing non-productive reaction cycles. Disrupting the TRiC-PFD interaction in vivo is strongly deleterious, leading to accumulation of amyloid aggregates
-
prefoldin
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
also PFD or GimC, TRiC subunits and co-chaperones such as prefoldin and phosducin-like proteins interact with the substrate to assist the overall folding process in a substrate-specific manner. The PFD molecule acts as a mediator working in tandem with a TRiC chaperonin to assemble into a chaperone complex via electrostatic inetractions. This complex has the crucial function of accurately folding other nascent proteins. PhLP2A binds to the open TRiC chamber and modulates TRiC-PFD interactions
-
prefoldin
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
PFD or GimC, TRiC subunits and co-chaperones such as prefoldin and phosducin-like proteins interact with the substrate to assist the overall folding process in a substrate-specific manner. The PFD molecule acts as a mediator working in tandem with a TRiC chaperonin to assemble into a chaperone complex via electrostatic interactions. This complex has the crucial function of accurately folding other nascent proteins
-
prefoldin
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
deliver nascent actin and tubulin to CCT for folding. Prefoldin not only delivers actin to CCT, but also participates in the folding process to enhance CCT processivity and reduce actin aggregation. CCT-bound via two distinct conformations: a latched form in which prefoldin is bound but offset at an angle, and an engaged form in which the substrate binding chambers are aligned and the tentacles of prefoldin extend into the CCT folding chamber to modulate the substrate-binding surface
-
prefoldin
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
consists of six homologous subunits that associate in a structure that resembles a jelly fish, with a body made up of a double beta-barrel domain and six tentacles consisting of coiled-coils from each subunit
-
prefoldin
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
hexameric prefoldin chaperone
-
additional information
the group II CPNs do not require a GroES-like co-CPN but have a built-in lid that is composed of a helical protrusion in the apical domain. The rate of transfer of a substrate protein from PFD to CPN correlates with the strength of the PFD-CPN interaction
-
additional information
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
PhLP2A binds to the open TRiC chamber and modulates TRiC-PFD interactions
-
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
several co-chaperones of CCT have been identified that modulate its function and play important roles in folding certain substrates. These include prefoldin and the phosducin-like proteins (PhLPs). There are four mammalian PhLPs (PhLP1-PhLP4) known to be involved with CCT
-
additional information
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
Hsp40A chaperone
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K+
Mg2+
Mn2+
additional information
K+
ATPase activity of the two chaperonin subunits is dependent on the salt concentration. Among the ions examined, K+ are the most effective at enhancing the ATP hydrolysis activity of ApCpnA and ApCpnB. Activity is maximal at 200 mM K+
K+
required, the ATP hydrolysis rate is negligible in the absence of K+
Mg2+
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
required
Mg2+
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
required
Mg2+
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
required
Mg2+
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
required
Mg2+
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
required
Mg2+
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
required
Mg2+
F6T521; F6PJP5; G7MDZ6; A0A5F7ZBU8; A0A1D5Q8I4; I0FKJ8; A0A1D5RDC8; A0A5F7Z7P5
required
Mg2+
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
required
Mg2+
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
required
Mg2+
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
required
Mg2+
with the addition of Mg2+ ion protection activity on inorganic phosphatase from thermal inactivation at 85°C and 110°C increases 2fold compared with the addition of enzyme alone
Mg2+
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
required
additional information
the ATPase activity of the two chaperonin subunits is dependent on the salt concentration. Potassium ions are the most effective at enhancing the ATP hydrolysis activity of ApCpnA and ApCpnB, activity is maximal at 200 mM K+
additional information
the ATPase activity of the two chaperonin subunits is dependent on the salt concentration. Potassium ions are the most effective at enhancing the ATP hydrolysis activity of ApCpnA and ApCpnB, activity is maximal at 200 mM K+
additional information
the ATPase activity of the two chaperonin subunits is dependent on the salt concentration. Potassium ions are the most effective at enhancing the ATP hydrolysis activity of ApCpnA and ApCpnB, activity is maximal at 200 mM K+
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
AMP-PNP
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
ADP (or ATP, with a minor likelihood) remains bound on the CCT6 side of TRiC in the presence of excess AMP-PNP (10 mM), although some of the ADP may be replaced by AMP-PNP
HSF1A
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
a cell permeable TRiC/CCT small molecule inhibitor. HSF1A exhibits a dose-dependent inhibitory effect on production of LCMV infectious progeny within a range of HSF1A concentrations that has modest effects in cell viability
-
prefoldin
-
inhibits the GFP protein refolding by interacting with intermediates
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
prefoldin
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
PFD, is required for protein substrate folding
-
prefoldin
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
PFD or GIMc, binds directly to TRiC through an electrostatic pivot, suggesting a direct mechanism of substrate transfer. Prefoldin maintains tubulin in a highly unstructured state and directly transfers substrate into the TRiC chamber
-
prefoldin
-
a molecular chaperone that can stabilize tentatively nascent polypeptide chains or non-native forms of mainly cytoskeletal proteins, which are subsequently delivered to group II chaperonin to accomplish their precise folding, effects of Pyrococcus furiosus prefoldin on the refolding reactions of Pyrococcus furiosus citrate synthase and Aequorea enhanced green fluorescence protein differ in the presence or absence of Pyrococcus furiosus chaperonin, PfuCPN. Both prefoldin and chaperonin CPN interact with Pyrococcus furiosus citrate synthase and Aequorea enhanced green fluorescence protein refolding intermediates. Recombinant expression of prefoldin in Escherichia coli
-
prefoldin
the enzyme is not effective in the refolding of isopropylmalate dehydrogenase, the refolding efficiency is enhanced by the cooperation of the enzyme with Pyrococcus prefoldin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma of Lung
Targeting ?-tubulin/CCT-? complex induces apoptosis and suppresses migration and invasion of highly metastatic lung adenocarcinoma.
Alzheimer Disease
The TRiC/CCT chaperone is implicated in Alzheimer's disease based on patient GWAS and an RNAi screen in A?-expressing Caenorhabditis elegans.
Anthrax
CCT chaperonin complex is required for efficient delivery of anthrax toxin into the cytosol of host cells.
Astrocytoma
Analysis of the antibody repertoire of astrocytoma patients against antigens expressed by gliomas.
Autoimmune Diseases
Chaperonin-containing T-complex Protein 1 Subunit ? Serves as an Autoantigen Recognized by Human V?2 ?? T Cells in Autoimmune Diseases.
Bardet-Biedl Syndrome
MKKS/BBS6, a divergent chaperonin-like protein linked to the obesity disorder Bardet-Biedl syndrome, is a novel centrosomal component required for cytokinesis.
Blindness
Mutation in the Zebrafish cct2 Gene Leads to Abnormalities of Cell Cycle and Cell Death in the Retina: A Model of CCT2-Related Leber Congenital Amaurosis.
Breast Neoplasms
Systematic Characterization of Expression Profiles and Prognostic Values of the Eight Subunits of the Chaperonin TRiC in Breast Cancer.
Breast Neoplasms
Two members of the TRiC chaperonin complex, CCT2 and TCP1 are essential for survival of breast cancer cells and are linked to driving oncogenes.
Carcinogenesis
Subcellular and functional proteomic analysis of the cellular responses induced by Helicobacter pylori.
Carcinoma
Expression and significance of p53 and mdm2 in atypical intestinal metaplasia and gastric carcinoma.
Carcinoma
Expression of E-cadherin and beta-catenin in gastric carcinoma and its correlation with the clinicopathological features and patient survival.
Carcinoma
Gatric carcinoma. A prospective study of tumour differentiation correlated to surgical procedures and survival rate.
Carcinoma, Hepatocellular
Prognostic Power of a Chaperonin Containing TCP-1 Subunit Genes Panel for Hepatocellular Carcinoma.
Carcinoma, Hepatocellular
The TCP1 ring complex is associated with malignancy and poor prognosis in hepatocellular carcinoma.
Cardiovascular Diseases
Chaperonin-containing TCP-1 complex directly binds to the cytoplasmic domain of the LOX-1 receptor.
Colonic Neoplasms
A novel peptide specifically targeting the vasculature of orthotopic colorectal cancer for imaging detection and drug delivery.
Colorectal Neoplasms
A novel peptide specifically targeting the vasculature of orthotopic colorectal cancer for imaging detection and drug delivery.
Colorectal Neoplasms
A novel vascular-targeting peptide for gastric cancer delivers low-dose TNF? to normalize the blood vessels and improve the anti-cancer efficiency of 5-fluorouracil.
Colorectal Neoplasms
Modulated T-complex protein 1 ? and peptidyl-prolyl cis-trans isomerase B are two novel indicators for evaluating lymph node metastasis in colorectal cancer: Evidence from proteomics and bioinformatics.
Colorectal Neoplasms
Vascular-targeted TNF? and IFN? inhibits orthotopic colorectal tumor growth.
Colorectal Neoplasms
Vascular-targeted TNF? improves tumor blood vessel function and enhances antitumor immunity and chemotherapy in colorectal cancer.
Down Syndrome
Expression patterns of chaperone proteins in cerebral cortex of the fetus with Down syndrome: dysregulation of T-complex protein 1.
Epstein-Barr Virus Infections
Proteomics Analysis of Gastric Epithelial AGS Cells Infected with Epstein-Barr Virus.
Glioma
Analysis of the antibody repertoire of astrocytoma patients against antigens expressed by gliomas.
Hepatitis C
Chaperonin TRiC/CCT participates in replication of hepatitis C virus genome via interaction with the viral NS5B protein.
Hereditary Sensory and Autonomic Neuropathies
Structure of the human TRiC/CCT Subunit 5 associated with hereditary sensory neuropathy.
Infections
Identification of candidate protein markers of Bovine Parainfluenza Virus Type 3 infection using an in vitro model.
Infections
[Preliminary investigation of Helicobacter pylori infection in Linqu County of Shandong province]
Leber Congenital Amaurosis
Mutation in the Zebrafish cct2 Gene Leads to Abnormalities of Cell Cycle and Cell Death in the Retina: A Model of CCT2-Related Leber Congenital Amaurosis.
Leukemia, Myeloid, Acute
Chaperonin TRiC/CCT Recognizes Fusion Oncoprotein AML1-ETO through Subunit-Specific Interactions.
Lymphadenopathy
Silencing P2X7 receptor downregulates the expression of TCP-1 involved in lymphoma lymphatic metastasis.
Lymphatic Metastasis
Modulated T-complex protein 1 ? and peptidyl-prolyl cis-trans isomerase B are two novel indicators for evaluating lymph node metastasis in colorectal cancer: Evidence from proteomics and bioinformatics.
Lymphatic Metastasis
Silencing P2X7 receptor downregulates the expression of TCP-1 involved in lymphoma lymphatic metastasis.
Lymphoma
Silencing P2X7 receptor downregulates the expression of TCP-1 involved in lymphoma lymphatic metastasis.
Neoplasm Metastasis
Modulated T-complex protein 1 ? and peptidyl-prolyl cis-trans isomerase B are two novel indicators for evaluating lymph node metastasis in colorectal cancer: Evidence from proteomics and bioinformatics.
Neoplasm Metastasis
Silencing P2X7 receptor downregulates the expression of TCP-1 involved in lymphoma lymphatic metastasis.
Neoplasms
?133p53? isoform pro-invasive activity is regulated through an aggregation-dependent mechanism in cancer cells.
Neoplasms
A novel peptide specifically targeting the vasculature of orthotopic colorectal cancer for imaging detection and drug delivery.
Neoplasms
A novel vascular-targeting peptide for gastric cancer delivers low-dose TNF? to normalize the blood vessels and improve the anti-cancer efficiency of 5-fluorouracil.
Neoplasms
Chaperonin Containing-TCP-1 Protein Level in Breast Cancer Cells Predicts Therapeutic Application of a Cytotoxic Peptide.
Neoplasms
Chaperonin-Containing TCP1 Complex (CCT) Promotes Breast Cancer Growth Through Correlations With Key Cell Cycle Regulators.
Neoplasms
Diverse effects of mutations in exon II of the von Hippel-Lindau (VHL) tumor suppressor gene on the interaction of pVHL with the cytosolic chaperonin and pVHL-dependent ubiquitin ligase activity.
Neoplasms
Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC.
Neoplasms
Gatric carcinoma. A prospective study of tumour differentiation correlated to surgical procedures and survival rate.
Neoplasms
Identification of the TRiC/CCT substrate binding sites uncovers the function of subunit diversity in eukaryotic chaperonins.
Neoplasms
Matrine induces papillary thyroid cancer cell apoptosis in vitro and suppresses tumor growth in vivo by downregulating miR-182-5p.
Neoplasms
Molecular and Clinical Characterization of CCT2 Expression and Prognosis via Large-Scale Transcriptome Profile of Breast Cancer.
Neoplasms
Multiple malignant primary neoplasms in patients with gatric neoplasms in the health district of León.
Neoplasms
Systematic Characterization of Expression Profiles and Prognostic Values of the Eight Subunits of the Chaperonin TRiC in Breast Cancer.
Neoplasms
The Hsp70 and TRiC/CCT chaperone systems cooperate in vivo to assemble the von Hippel-Lindau tumor suppressor complex.
Neoplasms
The TCP1 ring complex is associated with malignancy and poor prognosis in hepatocellular carcinoma.
Neoplasms
Tumorigenic mutations in VHL disrupt folding in vivo by interfering with chaperonin binding.
Neoplasms
Understanding the Molecular Mechanism of miR-877-3p Could Provide Potential Biomarkers and Therapeutic Targets in Squamous Cell Carcinoma of the Cervix.
Neoplasms
Vascular-targeted TNF? improves tumor blood vessel function and enhances antitumor immunity and chemotherapy in colorectal cancer.
Neoplasms
[Effects of RNA interference of CTHRC1 on proliferation and apoptosis of thyroid papillary cancer TCP-1 cells in vitro].
Neoplasms
[Preliminary investigation of Helicobacter pylori infection in Linqu County of Shandong province]
Neurodegenerative Diseases
Sirt1s beneficial roles in neurodegenerative diseases - a chaperonin containing TCP-1 (CCT) connection?
Neurofibromatoses
Heat shock factor 1 (HSF1)-targeted anticancer therapeutics: overview of current preclinical progress.
Neurofibromatosis 1
Heat shock factor 1 (HSF1)-targeted anticancer therapeutics: overview of current preclinical progress.
Papillomavirus Infections
Human Papillomavirus infection requires the CCT Chaperonin Complex.
Pleural Effusion
Identification of 10 Candidate Biomarkers Distinguishing Tuberculous and Malignant Pleural Fluid by Proteomic Methods.
Pleural Effusion, Malignant
Identification of 10 Candidate Biomarkers Distinguishing Tuberculous and Malignant Pleural Fluid by Proteomic Methods.
Pulmonary Disease, Chronic Obstructive
Effects of genetic variations in Acads gene on the risk of chronic obstructive pulmonary disease.
Starvation
Regeneration in starved planarians depends on TRiC/CCT subunits modulating the unfolded protein response.
Stomach Diseases
Subcellular and functional proteomic analysis of the cellular responses induced by Helicobacter pylori.
Stomach Neoplasms
A novel vascular-targeting peptide for gastric cancer delivers low-dose TNF? to normalize the blood vessels and improve the anti-cancer efficiency of 5-fluorouracil.
Stomach Neoplasms
Chaperonin containing TCP-1 subunit 3 is critical for gastric cancer growth.
Stroke
A gradient of ATP affinities generates an asymmetric power stroke driving the chaperonin TRIC/CCT folding cycle.
Teratozoospermia
T-complex protein 1 subunit zeta-2 (CCT6B) deficiency induces murine teratospermia.
Thyroid Neoplasms
Effect of Interferon-? on the Basal and the TNF?-Stimulated Secretion of CXCL8 in Thyroid Cancer Cell Lines Bearing Either the RET/PTC Rearrangement Or the BRAF V600e Mutation.
Zika Virus Infection
TRiC/CCT Complex, a Binding Partner of NS1 Protein, Supports the Replication of Zika Virus in Both Mammalians and Mosquitoes.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
kinetic analysis, stopped-flow fluorometry and stopped-flow small-angle X-ray scattering and ATP dissociation constants of wild-type and mutant enzymes. Allosteric communication in the group II chaperonins lies only in the intra-ring contact regions, which are located entirely within the equatorial domains. No cooperativity in ATP binding
-
additional information
additional information
kinetic analysis, stopped-flow fluorometry and stopped-flow small-angle X-ray scattering and ATP dissociation constants of wild-type and mutant enzymes. Allosteric communication in the group II chaperonins lies only in the intra-ring contact regions, which are located entirely within the equatorial domains. No cooperativity in ATP binding
-
additional information
additional information
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
transient kinetic analysis of ATP hydrolysis by chaperonin CCT/TRiC, stopped-flow measurements. Two burst phases are observed, followed by a lag phase and then a linear steady-state phase of ATP hydrolysis. The burst phases are found to decrease with increasing ATP and K+ concentrations, thereby indicating that the apo state of CCT/TRiC is in equilibrium between several conformations and that conformational selection by ATP takes place before hydrolysis. The amplitude of the lag phase, which follows, decreases with increasing ATP concentrations, thus indicating that it reflects a transition between states with low affinity for ATP and a state with high affinity for ATP that is predominant under steady-state conditions. A kinetic model based on the data is suggested, in which CCT/TRiC is in equilibrium between a relatively large number of states that are distinguished kinetically, in agreement with its proposed sequential allosteric mechanism, overview
-
additional information
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics
-
additional information
additional information
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics
-
additional information
additional information
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics
-
additional information
additional information
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics
-
additional information
additional information
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics
-
additional information
additional information
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics
-
additional information
additional information
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics
-
additional information
additional information
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics
-
additional information
additional information
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics
-
additional information
additional information
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics
-
additional information
additional information
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics
-
additional information
additional information
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
chaperonins are machines driven by cycles of ATP binding and hydrolysis, and they all show strong interring negative cooperativity, meaning that the rings are generally in alternative states. Binding cooperativity is positive when the presence of an already bound ligand enhances the binding of another to the macromolecule. Within the CCT rings, there is weak positive cooperativity which may be concerted or sequential, and this aspect of the cooperativity effect is very difficult to distinguish kinetically using Hill coefficients of ATPase kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.4
7.5
7.4
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
ATPase assay and refolding assay at
8
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
refolding/ATPase assay at
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
30
37
4
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
refolding/ATPase
60
80
25
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
refolding assay at
30
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
ATPase assay at
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0 - 30
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
activity range, profile overview
30 - 90
activity range of wild-type and mutant enzymes, profiles overview
70 - 85
70°C: about 60% of maximal actiovity, 85°C: about 40% of maximal activity
70 - 95
70°C: about 70% of maximal activity, 95°C: about 50% of maximal activity
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Q9YDK6: alpha-subunit, Q9YA66: beta-subunit
SwissProt
brenda
genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
UniProt
brenda
genes cct-1 to cct-8 encoding subunits TCP-1-alpha, TCP-1-beta, TCP-1-gamma, TCP-1-delta, TCP-1-epsilon, TCP-1-zeta, TCP-1-eta, and TCP-1-theta
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
UniProt
brenda
genes CCT1-5, and 6-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
UniProt
brenda
genes CCT1-5, and 6-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
UniProt
brenda
genes CCT1-5, 6a, 7, and 8 encoding subunits CCT-alpha (TCP-1 protein), CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
UniProt
brenda
genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon or CCT5 isoform A, CCT-zeta, CCT-eta, and CCT-theta
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
UniProt
brenda
genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon or CCT5 isoform A, CCT-zeta, CCT-eta, and CCT-theta
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
UniProt
brenda
genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon or CCT5 isoform A, CCT-zeta, CCT-eta, and CCT-theta
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
UniProt
brenda
genes encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
UniProt
brenda
subunits LdTCP1alpha, LdTCP1beta, LdTCP1gamma, LdTCP1delta, LdTCP1epsilon, LdTCP1zeta, LdTCP1eta, and LdTCP1theta
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
UniProt
brenda
subunits LdTCP1alpha, LdTCP1beta, LdTCP1gamma, LdTCP1delta, LdTCP1epsilon, LdTCP1zeta, LdTCP1eta, and LdTCP1theta
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
UniProt
brenda
Leishmania donovani MHOM/IN/80
subunits LdTCP1alpha, LdTCP1beta, LdTCP1gamma, LdTCP1delta, LdTCP1epsilon, LdTCP1zeta, LdTCP1eta, and LdTCP1theta
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
UniProt
brenda
subunits CCT1, CCT2, CCT3, CCT4, CCT5, CCT6A, CCT7, and CCT8 or subunits TCP1alpha, TCP1beta, TCP1gamma, TCP1delta, TCP1epsilon, TCP1zeta, TCP1eta, and TCP1theta
F6T521; F6PJP5; G7MDZ6; A0A5F7ZBU8; A0A1D5Q8I4; I0FKJ8; A0A1D5RDC8; A0A5F7Z7P5
UniProt
brenda
genes CCT1-5, 6A, 7, and 8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
UniProt
brenda
genes CCT1-5, 6A, 7, and 8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
UniProt
brenda
thermosome subunits alpha and beta; KS-1
UniProt
brenda
Q9YDK6: alpha-subunit, Q9YA66: beta-subunit
SwissProt
brenda
genes CCT1-5, 6A, 7, and 8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
UniProt
brenda
genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
UniProt
brenda
subunits CCT1, CCT2, CCT3, CCT4, CCT5, CCT6A, CCT7, and CCT8
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
UniProt
brenda
genes CCT1-8 encoding subunits TCP-1-alpha, TCP-1-beta, TCP-1-gamma, TCP-1-delta, TCP-1-epsilon, TCP-1-zeta, TCP-1-eta, and TCP-1-theta
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
UniProt
brenda
subunits CCT1, CCT2, CCT3, CCT4, CCT5, CCT6, CCT7, and CCT8
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
UniProt
brenda
genes encoding subunits alpha, beta, gamma, delta, epsilon, zeta, eta, and theta
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
UniProt
brenda
subunits CCT1. CCT2, CCT3, CCT4, CCT5, CCT6, CCT7, and CCT8
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
UniProt
brenda
genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
UniProt
brenda
subunits CCT1, CCT2, CCT3, CCT4, CCT5, CCT6A, CCT7, and CCT8 or subunits TCP1alpha, TCP1beta, TCP1gamma, TCP1delta, TCP1epsilon, TCP1zeta, TCP1eta, and TCP1theta
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
UniProt
brenda
genes CCT1-8 encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta, CCT-eta, and CCT-theta
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
UniProt
brenda
subunits CCT1, CCT2, CCT3, CCT4, CCT5, CCT6A, CCT7, and CCT8 or subunits TCP1alpha, TCP1beta, TCP1gamma, TCP1delta, TCP1epsilon, TCP1zeta, TCP1eta, and TCP1theta
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
UniProt
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
-
brenda
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
brenda
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
brenda
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
-
brenda
F6T521; F6PJP5; G7MDZ6; A0A5F7ZBU8; A0A1D5Q8I4; I0FKJ8; A0A1D5RDC8; A0A5F7Z7P5
-
brenda
among all tested OSCC cells, SCC-15 and HSC-3 cell lines exhibit higher CCT6A expression
brenda
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
-
brenda
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
-
brenda
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
brenda
additional information
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
brenda
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
prothoracic gland PG, a steroidogenic organ, PG cells undergo approximately four rounds of endocycling
brenda
-
prothoracic gland PG, a steroidogenic organ, PG cells undergo approximately four rounds of endocycling
-
brenda
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
subunit LdTCP1epsilon displays an increased expression up to 2.7 and 1.8fold in the late log phase and stationary phase promastigotes and exhibits majorly vesicular localization
brenda
-
subunit LdTCP1epsilon displays an increased expression up to 2.7 and 1.8fold in the late log phase and stationary phase promastigotes and exhibits majorly vesicular localization
-
brenda
Leishmania donovani MHOM/IN/80
-
subunit LdTCP1epsilon displays an increased expression up to 2.7 and 1.8fold in the late log phase and stationary phase promastigotes and exhibits majorly vesicular localization
-
brenda
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
-
brenda
additional information
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
GaTRiC is consistently expressed at all temperatures
brenda
additional information
-
GaTRiC is consistently expressed at all temperatures
brenda
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
TRiC co-precipitated with recombinantly expressed FLAG-tagged AML1-ETO in HEK-293 cells, along with HSP70 and HSP90, while actin is not detected. AML1-ETO induction does not affect cell viability, nor does it change the levels of actin, HSP70, HSP90, or TRiC proteins
brenda
additional information
the optimum growth temperature of the parent organism is 35-40°C
brenda
additional information
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
CCT complexes are extracted from infected human erythrocyte cultures synchronized for maximum expression levels of CCT at the trophozoite stage of the parasite's asexual life cycle. The maximum transcript levels and expression levels of CCT1 and CCT8 subunits are in the trophozoite stage of the asexual life cycle, overview
brenda
additional information
-
thermophilic fungus, Chaetomium thermophilum, thrives optimally at 50-55°C
brenda
additional information
Thermococcus kodakarensis optimally grows at 85°C, gene disruptant strain DA1 (DELTAcpkA) shows decreased cell growth at 60°C
brenda
additional information
Thermococcus kodakarensis optimally grows at 85°C, gene disruptant strain DA1 (DELTAcpkA) shows decreased cell growth at 60°C
brenda
additional information
Thermococcus kodakarensis optimally grows at 85°C, gene disruptant strain DB1 (DELTAcpkB) shows decreased cell growth at 93°C
brenda
additional information
Thermococcus kodakarensis optimally grows at 85°C, gene disruptant strain DB1 (DELTAcpkB) shows decreased cell growth at 93°C
brenda
additional information
Thermococcus kodakarensis grows optimally at 85°C, the mutant strain DA4 (pyrF cpkA-E530G) grows as well as the parental KU216 (pyrF) strain at 60°C, clear correlation between the CpkA-type chaperonin gene copy number and growth temperature
brenda
additional information
Thermococcus kodakarensis grows optimally at 85°C, the mutant strain DA4 (pyrF cpkA-E530G) grows as well as the parental KU216 (pyrF) strain at 60°C, clear correlation between the CpkA-type chaperonin gene copy number and growth temperature
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
-
brenda
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
upon heat stress, human TRiC-alpha translocates from the cytosolic fraction and associates with the cytoskeleton
brenda
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
-
brenda
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
-
brenda
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
-
brenda
F6T521; F6PJP5; G7MDZ6; A0A5F7ZBU8; A0A1D5Q8I4; I0FKJ8; A0A1D5RDC8; A0A5F7Z7P5
cytosolic inclusions termed viroplasms, that allow the synthesis of virus genome segments and their encapsidation in the core shell, followed by the addition of the second layer of the virion. The viroplasms are composed of several viral proteins, including NSP5, which serves as the main building block. Microtubules, lipid droplets, and miRNA-7 are among the host components recruited in viroplasms. TRiC inhibition impairs viroplasm morphology and virus progeny
-
brenda
additional information
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
brenda
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
brenda
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
-
brenda
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
-
brenda
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
-
brenda
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
-
brenda
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
-
brenda
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
-
brenda
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
chaperonin TRiC forms an heterohexadecameric complex in the red blood cell (RBC) cytosol. The stress of parasite infection may lead to translocation of human TRiC subunits from the soluble to insoluble fraction. But the human TRiC-beta and -delta subunits remain in the soluble cytosolic fraction in iRBC. Human TRiC subunits alpha and delta are present in the cytosol of RBC, and this localization is unchanged upon parasite infection
brenda
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
mild distribution of LdTCP1epsilon inside cytosol but it is mainly localized and concentrated in some vesicular structure near the nucleus in each parasite. On the other hand, subunit LdTCP1gamma is distributed homogenously throughout the cytosol
brenda
-
mild distribution of LdTCP1epsilon inside cytosol but it is mainly localized and concentrated in some vesicular structure near the nucleus in each parasite. On the other hand, subunit LdTCP1gamma is distributed homogenously throughout the cytosol
-
brenda
Leishmania donovani MHOM/IN/80
-
mild distribution of LdTCP1epsilon inside cytosol but it is mainly localized and concentrated in some vesicular structure near the nucleus in each parasite. On the other hand, subunit LdTCP1gamma is distributed homogenously throughout the cytosol
-
brenda
F6T521; F6PJP5; G7MDZ6; A0A5F7ZBU8; A0A1D5Q8I4; I0FKJ8; A0A1D5RDC8; A0A5F7Z7P5
-
brenda
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
-
brenda
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
-
brenda
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
chaperonin TRiC forms an heterohexadecameric complex in the malaria parasite cytosol
brenda
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
-
brenda
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
subunit LdTCP1epsilon displays an increased expression up to 2.7 and 1.8fold in the late log phase and stationary phase promastigotes and exhibits majorly vesicular localization
brenda
-
subunit LdTCP1epsilon displays an increased expression up to 2.7 and 1.8fold in the late log phase and stationary phase promastigotes and exhibits majorly vesicular localization
-
brenda
Leishmania donovani MHOM/IN/80
-
subunit LdTCP1epsilon displays an increased expression up to 2.7 and 1.8fold in the late log phase and stationary phase promastigotes and exhibits majorly vesicular localization
-
brenda
additional information
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
mild distribution of LdTCP1epsilon inside cytosol but it is mainly localized and concentrated in some vesicular structure near the nucleus in each parasite
-
brenda
additional information
-
mild distribution of LdTCP1epsilon inside cytosol but it is mainly localized and concentrated in some vesicular structure near the nucleus in each parasite
-
-
brenda
additional information
Leishmania donovani MHOM/IN/80
-
mild distribution of LdTCP1epsilon inside cytosol but it is mainly localized and concentrated in some vesicular structure near the nucleus in each parasite
-
-
brenda
additional information
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
the plasmodial subunit theta can form high molecular weight complexes in the parasite soluble fraction
-
brenda
additional information
-
the plasmodial subunit theta can form high molecular weight complexes in the parasite soluble fraction
-
brenda
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
-
the enzyme belongs to the archetypal group II chaperonins. Group II chaperonins are found in archaea and the eukaryotic cytosol. They consist of two stacked rings, each composed of eight 50- to 60-kDa subunits, but do not have an obligate co-chaperone in the same manner as the group I chaperonins. Rather, they contain a built-in lid that closes the folding chamber and are thus competent to fold substrates in vitro without the assistance of accessory proteins. Group II chaperonins appear to be at the heart of a complex network of co-chaperones. The eukaryotic group II chaperonin, i.e. TRiC/CCT, differs from its simpler archaeal homologues in that it is composed of eight paralogous subunits, while in eukaryotic chaperonin, TRiC/CCT, each ring contains eight distinct, paralogous subunits occupying fixed positions in the complex
evolution
-
the enzyme belongs to the eukaryotic group II chaperonins. Group II chaperonins are found in archaea and the eukaryotic cytosol. They consist of two stacked rings, each composed of eight 50- to 60-kDa subunits, but do not have an obligate co-chaperone in the same manner as the group I chaperonins. Rather, they contain a built-in lid that closes the folding chamber and are thus competent to fold substrates in vitro without the assistance of accessory proteins. Group II chaperonins appear to be at the heart of a complex network of co-chaperones, e.g. the phosducin-like proteins that enhance TRiC-mediated folding of several substrates. The eukaryotic group II chaperonin, i.e. TRiC/CCT, differs from its simpler archaeal homologues in that it is composed of eight paralogous subunits, while in eukaryotic chaperonin, TRiC/CCT, each ring contains eight distinct, paralogous subunits occupying fixed positions in the complex
evolution
-
the enzyme belongs to the archetypal group II chaperonins. Group II chaperonins are found in archaea and the eukaryotic cytosol. They consist of two stacked rings, each composed of eight 50- to 60-kDa subunits, but do not have an obligate co-chaperone in the same manner as the group I chaperonins. Rather, they contain a built-in lid that closes the folding chamber and are thus competent to fold substrates in vitro without the assistance of accessory proteins. Group II chaperonins appear to be at the heart of a complex network of co-chaperones. The eukaryotic group II chaperonin, i.e. TRiC/CCT, differs from its simpler archaeal homologues in that it is composed of eight paralogous subunits, while in eukaryotic chaperonin, TRiC/CCT, each ring contains eight distinct, paralogous subunits occupying fixed positions in the complex
evolution
the enzyme belongs to the group II chaperonins, that play important roles in protein homeostasis in the eukaryotic cytosol and in Archaea
evolution
the enzyme belongs to the group II chaperonins, which are found in archaeal (thermosome of Thermoplasma acidophilum) and in eukaryotic (chaperonin-containing TCP-1 or CCT) species, have eight or nine subunits per ring made of two (thermosome) or eight (CCT) types of subunits. Subunit heterogeneity in group II chaperonins, found primarily within the apical domains, has important consequences for the functional specialization of ring components, role of heterogeneity in subunit dynamics. Nonconservation of intra-ring cooperativity among chaperonin classes, overview
evolution
the chaperonins of group II in the cytosol of archaea and eukaryotic cells share the three-domain subunit topology and cylindrical architecture with the group I chaperonins, EC 3.6.4.9, but function without a GroES-like cofactor
evolution
the chaperonins of group II in the cytosol of archaea and eukaryotic cells share the three-domain subunit topology and cylindrical architecture with the group I chaperonins, EC 3.6.4.9, but function without a GroES-like cofactor
evolution
the enzyme belongs to the group II chaperonins, group II consists of the archaeal (thermosomes) and eukaryotic cytosolic variants (CCT or TRiC). The structure is more complex for group II chaperonins compared to group I chaperonins, EC 3.6.4.9. Evolution of group II chaperonins via rapid multiple gene duplication, folding mechanism, phylogenetic analyses
evolution
the enzyme belongs to the group II chaperonins, group II consists of the archaeal (thermosomes) and eukaryotic cytosolic variants (CCT or TRiC). The structure is more complex for group II chaperonins compared to group I chaperonins, EC 3.6.4.9. Evolution of group II chaperonins via rapid multiple gene duplication, folding mechanism, phylogenetic analyses
evolution
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
the eukaryotic chaperonin family includes the type I chaperonin, HSP60, and the type II hetero-oligomeric chaperonin, TRiC (T-complex protein-1 ring complex, also known as CCT). Chaperones often function as large protein complexes that include other proteins called co-chaperones
evolution
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the eukaryotic chaperonin family includes the type I chaperonin, HSP60, and the type II hetero-oligomeric chaperonin, TRiC (T-complex protein-1 ring complex, also known as CCT). Chaperones often function as large protein complexes that include other proteins called co-chaperones
evolution
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
TRiC has evolved into a complex structurally divided into two sides whose nucleotide binding and ring closure occur in a staggered manner, thus making it a highly coordixadnated macromolecular machine
evolution
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
chaperonin TRiC is evolutionarily conserved
evolution
-
chaperonins are subdivided into two families, group I and group II chaperonins
evolution
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
the protein MreB structure is rearranged by a binding-induced expansion mechanism in TRiC, GroEL and GroES. These results are quantitatively comparable to the structural rearrangements found during the interaction of beta-actin with GroEL and TRiC, indicating that the mechanism of chaperonins is conserved during evolution
evolution
chaperonins (CPNs) are subdivided into group I and group II. Group I CPNs are present in bacteria and in the organelles of eukaryotes. Group II CPNs exist in the cytosol of archaea and eukaryotes
evolution
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
co-evolution of CCT and the eukaryotic cytoskeleton, overview
evolution
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
co-evolution of CCT and the eukaryotic cytoskeleton, overview
evolution
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
co-evolution of CCT and the eukaryotic cytoskeleton, overview
evolution
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
co-evolution of CCT and the eukaryotic cytoskeleton, overview
evolution
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
co-evolution of CCT and the eukaryotic cytoskeleton, overview
evolution
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
co-evolution of CCT and the eukaryotic cytoskeleton, overview
evolution
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
co-evolution of CCT and the eukaryotic cytoskeleton, overview
evolution
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
three BBS proteins which have homology to chaperonins, BBS6, BBS10 and BBS12, and a sub-complex of CCT proteins (CCT1, 2, 3, 4, 5 and 8) mediate the association of two beta-propeller domain-containing proteins, BBS7 and BBS2, during the assembly process of the BBSome. BBS6, -10 and -12 are vertebrate-specific proteins and it may be an evolutionary connection that one of the two absent CCT subunits in the BBS-CCT complex, CCT6, has a vertebrate-specific isoform, CCT6B, which is abundant in testis CCT. CCT6 self-interacts across the CCT rings which probably permits isoform interchange, and therefore, it is possible that one of the BBS subunits has hijacked this mechanism and is able to slot into the CCT6 position in the CCT ring system. Co-evolution of CCT and the eukaryotic cytoskeleton, overview
evolution
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
co-evolution of CCT and the eukaryotic cytoskeleton, overview
evolution
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
co-evolution of CCT and the eukaryotic cytoskeleton, overview
evolution
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
co-evolution of CCT and the eukaryotic cytoskeleton, overview
evolution
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
co-evolution of CCT and the eukaryotic cytoskeleton, overview
evolution
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
subunit LdTCP1epsilon exhibits significant differences in the primary structure as compared to LdTCP1gamma and is evolutionary close to LdTCP1 zeta subunit, phylogenetic analysis
evolution
-
chaperonins are a highly conserved subgroup of chaperones that consists of two stacked seven- to nine-membered rings. Chaperonins are further divided into two major subtypes, group I and group II. Both share a similar domain arrangement, in that each subunit consists of three domains
evolution
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the CCT/TRiC subunit arrangement arose early in the evolution of eukaryotic cells and is universally conserved throughout the domain, allowing for a dramatic increase in diversity and specificity in substrate interactions over bacterial or archaeal chaperonins that have just one or two isoforms in their ring structures. The emergence of CCT has been likely a key factor in the rise of eukaryotic proteome complexity as CCT interacts with an estimated 10% of the cytosolic proteome
evolution
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
the CCT/TRiC subunit arrangement arose early in the evolution of eukaryotic cells and is universally conserved throughout the domain, allowing for a dramatic increase in diversity and specificity in substrate interactions over bacterial or archaeal chaperonins that have just one or two isoforms in their ring structures. The emergence of CCT has been likely a key factor in the rise of eukaryotic proteome complexity as CCT interacts with an estimated 10% of the cytosolic proteome
evolution
chaperonin containing TCP1 subunit 6A (CCT6A), belongs to the chaperonin containing TCP1 (CCT) family
evolution
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
evolutionarily, chaperonins are classified into two different groups, group I and group II, based on their architecture and folding mechanism. Group II chaperonins consist of the archaeal chaperonins called thermosomes and the eukaryotic chaperonin T-complex protein-1 ring complex (TRiC/CCT). The different CCT subunit genes are products of duplication events occurring early during the evolution of eukaryotic cells, phylogenetic analysis. These products independently diverged with distinct functions. Although the CCT subunits carry only 27%-39% identical sequences, their secondary structures are very similar
evolution
-
subunit LdTCP1epsilon exhibits significant differences in the primary structure as compared to LdTCP1gamma and is evolutionary close to LdTCP1 zeta subunit, phylogenetic analysis
-
evolution
-
co-evolution of CCT and the eukaryotic cytoskeleton, overview
-
evolution
-
the enzyme belongs to the group II chaperonins, that play important roles in protein homeostasis in the eukaryotic cytosol and in Archaea
-
evolution
-
the chaperonins of group II in the cytosol of archaea and eukaryotic cells share the three-domain subunit topology and cylindrical architecture with the group I chaperonins, EC 3.6.4.9, but function without a GroES-like cofactor
-
evolution
-
co-evolution of CCT and the eukaryotic cytoskeleton, overview
-
evolution
-
the CCT/TRiC subunit arrangement arose early in the evolution of eukaryotic cells and is universally conserved throughout the domain, allowing for a dramatic increase in diversity and specificity in substrate interactions over bacterial or archaeal chaperonins that have just one or two isoforms in their ring structures. The emergence of CCT has been likely a key factor in the rise of eukaryotic proteome complexity as CCT interacts with an estimated 10% of the cytosolic proteome
-
evolution
-
co-evolution of CCT and the eukaryotic cytoskeleton, overview
-
evolution
-
the enzyme belongs to the group II chaperonins, which are found in archaeal (thermosome of Thermoplasma acidophilum) and in eukaryotic (chaperonin-containing TCP-1 or CCT) species, have eight or nine subunits per ring made of two (thermosome) or eight (CCT) types of subunits. Subunit heterogeneity in group II chaperonins, found primarily within the apical domains, has important consequences for the functional specialization of ring components, role of heterogeneity in subunit dynamics. Nonconservation of intra-ring cooperativity among chaperonin classes, overview
-
evolution
-
the enzyme belongs to the group II chaperonins, group II consists of the archaeal (thermosomes) and eukaryotic cytosolic variants (CCT or TRiC). The structure is more complex for group II chaperonins compared to group I chaperonins, EC 3.6.4.9. Evolution of group II chaperonins via rapid multiple gene duplication, folding mechanism, phylogenetic analyses
-
evolution
Leishmania donovani MHOM/IN/80
-
subunit LdTCP1epsilon exhibits significant differences in the primary structure as compared to LdTCP1gamma and is evolutionary close to LdTCP1 zeta subunit, phylogenetic analysis
-
malfunction
gene disruptant strain DA1 (DELTAcpkA) shows decreased cell growth at 60°C, DA1 cells grow optimally in minimal medium only in the presence of tryptophan but hardly grow in the absence of tryptophan at 60°C. A lesion of functional indole-3-glycerol-phosphate synthase, TrpC, is caused by cpkA disruption, resulting in tryptophan auxotrophy
malfunction
gene disruptant strain DB1 (DELTAcpkB) shows decreased cell growth at 93°C
malfunction
introduction of single mutations into the CpkA C-terminal region show that a single base substitution E530G allows the organism to adapt to a lower temperature
malfunction
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
knockdown of TRiC in HEPG2 cells reduces their sensitivity to interleukin-6 induced STAT3 activation
malfunction
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
RNAi knockdown of each TRiC subunit substantially reduces the levels of intracellular reovirus proteins, providing evidence that TRiC is required for the production or stabilization of viral polypeptides
malfunction
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
reduction of subunit CCT4 results in growth defects by affecting both cell size and proliferation. Loss of CCT4 causes preferential cell death anterior to the morphogenetic furrow in the eye disc and within wing pouch in the wing disc. Depletion of any CCT subunit in the eye disc results in headless phenotype and loss-of-function phenotypes by disrupting the function of the CCT complex in vivo. Overgrowth by active TOR signaling is suppressed by CCT RNAi. Loss of CCT leads to decreased phosphorylation of S6K and S6 while increasing phosphorylation of Akt. Insulin/TOR signaling is also necessary and sufficient for promoting CCT complex transcription. Reduction of the CCT complex leads to decreases in phospho-S6K and phospho-S6 while increasing phospho-Akt. CCT4 RNAi in the posterior wing disc under en-Gal4 causes early pupal lethality. Wing discs from en>CCT4 RNAi show almost complete loss of the posterior compartment marked by en>GFP. In comparison to control en>+, CCT4-depleted larvae show considerable developmental delay during its growth up to the third-instar stage, eventually resulting in pupal lethality. Consistent with the expression of ptc-Gal4 in the salivary gland, CCT4 RNAi reduced the size of the gland compared with control. In addition, knockdown of CCT4 in the wing pouch region of the developing wing disc under MS1096-Gal4 leads to loss of adult wing
malfunction
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
knockdown of TRiC subunits in the prothoracic gland (PG) causes a prolonged mitotic period, probably due to impaired nuclear translocation of Fizzy-related (Fzr), which also causes loss of ecdysteroidogenic activity. Fzr mediates downregulation of mitotic cyclins
malfunction
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
in zebrafish, TRiC loss causes specific defects in sarcomere and neurite formation. A missense mutation in the CCT5 subunit of TRiC leads to skeletal muscle defects, mutant cct5tf212b. Loss of individual subunits abolishes Z-disk localization. Expression of GFP-tagged subunit CCT3 in the musculature significantly ameliorates the muscle integrity deficits of transgenic cct3sa1761 homozygotes, as evaluated by birefringence analysis, indicating that the fusion protein is functional and integrated normally into TRiC. All cct mutants show retina degeneration, except for cct5tf212b, phenotypes, overview
malfunction
the wild-type organism shows reduced growth under GroES/GroEL-limiting conditions. Cells are transformed with plasmids expressing Mm-cpn, Mm-cpn-M223I, and Mm-cpn-K216E and grown at 26°C, 30°C, and 37°C in the presence of sucrose. Apart from the positive control, growth is observed only for cells expressing the mutant Mm-cpn-K216E. These cells show distinct visible colonies after 3 days at 26°C and 30°C in numbers comparable to those observed for cells expressing GroEL. Cells expressing Mm-cpn-K216E also form visible colonies at 37°C after 5 days. Loss of ATPase activity by mutation D386A severely affects the complementing ability of the wild-type and mutant Mm-cpn proteins
malfunction
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
mutations of subunit CCT5 are involved in sensory neuropathy. Mutation H147R of subunit CCT5 is involved in hereditary sensory neuropathies that show degeneration of the fibres in the sensory periphery neurons
malfunction
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
gene deletion of the gene encoding cofactor phosducin I in Dictyostelium discoideum causes inhibition of G-protein signalling and Gbetagamma dimer formation, deletion of the phosducin II gene is lethal with cell division collapse after 5 days, while deletion of phosducin IIII gene causes no phenotype
malfunction
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
deletion of the phosducin III gene causes embryo division arrest with astral microtubule defects
malfunction
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
mutations of subunit CCT5 are involved in sensory neuropathy. Mutation C450Y of subunit CCT4 is involved in hereditary sensory neuropathies that show degeneration of the fibres in the sensory periphery neurons
malfunction
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
knockdown of cct1 and cct2 in zebrafish leads to BBS-like phenotypes
malfunction
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
knockdown of the CCT8/theta subunit leads to a severe growth defect in asexual development but does not alter protein trafficking in the red blood cell compartment
malfunction
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
disrupting the TRiC-PFD interaction in vivo is strongly deleterious, leading to accumulation of amyloid aggregates
malfunction
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
three categories of residue substitutions are found in alpha, beta, and gamma subunits: (i) bulky/polar side chains to alanine or valine, (ii) charged residues to alanine, and (iii) isoleucine to valine that is expected to increase intramolecular flexibility within the GaTRiC. The residue substitutions observed in the built structures possibly affect the hydrophobic, hydrogen bonds, and ionic and aromatic interactions which lead to an increase in structural flexibility
malfunction
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
knockdown of the PfTRiC-theta subunit is lethal, the lethality is not due to a change in protein export into the host red blood cell (RBC) compartment. Loss of the PfTRiC complex does not alter export of PfSBP1 or PfREX1. The PfTRiC-theta-MYC clones of teh engineered regulatable line retain between 4 and 10 aptamer elements. The degree of regulation of expression correlates with the number of aptamers in the array, and knockdown reveals that PfTRiC-theta is essential for asexual parasite growth. But loss of one subunit in the heterohexadecamer disrupts formation of the entire complex
malfunction
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
knockdown of the PfTRiC-theta subunit is lethal, the lethality is not due to a change in protein export into the host red blood cell (RBC) compartment
malfunction
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
RNAi-mediated knockdown targeting CCT2 inhibits growth and colony formation of SUM-52 breast cancer cells
malfunction
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
cardiac-specific knockdown of CCT chaperonin significantly shortens lifespans. Additionally, disruption of circadian rhythm yields further deterioration of cardiac function of hypomorphic CCT mutants. CCT knockdown leads to disorganization of cardiac actin- and myosin-containing myofibrils and severe physiological dysfunction, including restricted heart diameters, elevated cardiac dysrhythmia and compromised cardiac performance
malfunction
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
pharmacological inhibition of TRiC/CCT complex function, or RNAi-mediated knockdown of TRiC/CCT complex subunits, inhibits mammarenavirus lymphocytic choriomeningitis virus (LCMV) multiplication in human cells. Pharmacological inhibition of the TRIC/CCT complex also restricts multiplication of the live-attenuated vaccine candidates Candid#1 and ML29 of the hemorrhagic fever causing Junin (JUNV) and Lassa (LASV) mammarenaviruses, respectively
malfunction
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
CCT depletion results in a 65% decrease in mTOR immunoprecipitation with corresponding decreases in mLST8 and Raptor co-immunoprecipitation. This decrease in mTORC1 formation can be attributed to similar decreases in mTOR, mLST8, and Raptor expression upon CCT depletion. CCT depletion does not change mTOR immunoprecipitation, but it causes a decrease in mLST8 (50%) and mSIN1 (30%) co-immunoprecipitation in the case of mTORC2. Subunits with residual nucleotide-binding and low-ATP utilization reside on the CCT6 side of the ring, roughly the same side that binds mLST8
malfunction
F6T521; F6PJP5; G7MDZ6; A0A5F7ZBU8; A0A1D5Q8I4; I0FKJ8; A0A1D5RDC8; A0A5F7Z7P5
inhibition of TRiC hampers viroplasm formation and RV replication. Chemical inhibition of TRiC and silencing of its subunits drastically reduces virus progeny production. TRiC inhibition results in defective virus particles lacking genome segments and polymerase complex (VP1/VP3). Inhibition of TRiC derives from a shortage of TLPs in the endoplasmic reticulum surrounding viroplasms and, most importantly, DLPs/TLPs lacking VP1/VP3 complex and dsRNA genome segments, thus, TRiC inhibition produces empty DLP/TLPs
malfunction
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
mutagenesis of the active sites of subunits CCT6 and CCT8 has little to no effect on CCT activity or cell viability in yeast, suggesting that they do not contribute to ATP hydrolysis
malfunction
CCT6A overexpression increases cell proliferation, invasion, sphere formation, CD133, and Sox2 expression, but decreases cell apoptosis, while CCT6A knockout exhibits an opposite effect on the above indexes in oral squamous cell carcinoma cells
malfunction
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
TRiC/CCT dysfunction leads to various clinical disorders, mechanisms e.g. of apoptosis, metastasis, and drug resistance, detailed overview
malfunction
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
depletion of CCT results in increased A3A mutational activity and A3A-induced DNA damage and cytotoxicity. Enrichment of A3A mutational signatures in cancers with silencing mutations in CCT subunit genes in canver genomes
malfunction
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
disruption of the TRiC/CCT by knocking down CCT1 or CCT5 leads to misfolding and lysosomal degradation of WDTC1, knockdown of CCT1 or CCT5 eliminates the inhibitory effect of WDTC1 on adipogenesis
malfunction
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
disruption of the TRiC/CCT by knocking down CCT1 or CCT5 leads to misfolding and lysosomal degradation of WDTC1, knockdown of CCT1 or CCT5 eliminates the inhibitory effect of WDTC1 on adipogenesis
malfunction
-
knockdown of TRiC subunits in the prothoracic gland (PG) causes a prolonged mitotic period, probably due to impaired nuclear translocation of Fizzy-related (Fzr), which also causes loss of ecdysteroidogenic activity. Fzr mediates downregulation of mitotic cyclins
-
malfunction
-
mutations of subunit CCT5 are involved in sensory neuropathy. Mutation C450Y of subunit CCT4 is involved in hereditary sensory neuropathies that show degeneration of the fibres in the sensory periphery neurons
-
malfunction
-
mutagenesis of the active sites of subunits CCT6 and CCT8 has little to no effect on CCT activity or cell viability in yeast, suggesting that they do not contribute to ATP hydrolysis
-
metabolism
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
chaperone network involving HSP70, HSP90, and TRiC, overview
metabolism
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
chaperone network involving HSP70, HSP90, and TRiC, overview
metabolism
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
Vaccinia-related kinase 2 controls the stability of the eukaryotic chaperonin TRiC/CCT by inhibiting the deubiquitinating enzyme USP25. VRK2 function in the negative regulation of TRiC
metabolism
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
comparison of the mechanisms of action of the GroEL/GroES and the TRiC chaperonin systems on MreB client protein variants extracted from Escherichia coli. MreB is a homologue to actin in prokaryotes
metabolism
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
CCT-actin system, overview
metabolism
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
CCT-actin system, overview
metabolism
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
CCT-actin system, overview
metabolism
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
CCT-actin system, overview. Interactions between CCT, actin and Plp2p in yeast: the actin map shows the CCT-binding sites, I, II and III and hinges, and the essential actin-binding D244 residue located in actin subdomain 4, which biochemically cross-links to the CCT8 subunit. Yeast actin (ACT1) binding to yeast CCT induces protease resistance in Cct4p and Cct8p. The PLP2 component shows its interactions with CCT subunits, CCT1, CCT4 and CCT8
metabolism
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
CCT-actin system, overview
metabolism
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
CCT-actin system, overview
metabolism
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
CCT-actin system, overview
metabolism
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
pathway of actin folding directed by the eukaryotic chaperonin TRiC, overview
metabolism
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the TCP1 subunit of TRiC is regulated by FGFR2, necessary for proliferation of breast cancer cells and associated with poor overall survival of breast cancer patients. FGFR2 signals through PI3K and Akt to regulate TCP1 expression, this signaling does not require mTOR activity
metabolism
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
proper cellular proteostasis, essential for viability, requires a network of chaperones and cochaperones. ATP-dependent chaperonin TRiC/CCT partners with cochaperones prefoldin (PFD) and phosducin-like proteins (PhLPs) to facilitate folding of essential eukaryotic proteins. Phosducin-like PhLP2A-chaperonin TRiC cooperation during the ATP-driven folding cycle, ATP-driven PhLP2A structural rearrangement cycle within the TRiC chamber to facilitate folding
metabolism
F6T521; F6PJP5; G7MDZ6; A0A5F7ZBU8; A0A1D5Q8I4; I0FKJ8; A0A1D5RDC8; A0A5F7Z7P5
recruitment of TRiC chaperonin in rotavirus viroplasms correlates with virus replication. Tandem mass spectrometry identifies all eight subunits of the tailless complex polypeptide I ring complex (TRiC) in viroplasms of infected cells. TRiC is brought into viroplasms and wraps around newly formed double-layered virus particles. TRiC is critical for RV replication by controlling dsRNA genome segment synthesis, particularly negative-sense single-stranded RNA. Viral particle VP2 is shown to be essential for recruiting TRiC in viroplasms and preserving their globular morphology
metabolism
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the most abundant substrates are the cytoskeletal proteins actin and tubulin, which must be folded by CCT prior to forming microfilament and microtubule structures
metabolism
determination of CCT6A mediated pathways in oral squamous cell carcinoma (OSCC) cells , overview
metabolism
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the tubulin folding pathway is directed by human chaperonin TRiC/CCT
metabolism
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
versatile roles of TRiC/CCT in biological processes from the perspective of the protein interactome, e.g. effect of TRiC/CCT on metabolic reprogramming in oesophageal squamous cell carcinoma by CCT4, overview
metabolism
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
APOBEC3 cytidine deaminases are implicated as the cause of a prevalent somatic mutation pattern found in cancer genomes. The APOBEC3A (A3A) enzyme is the most potent deaminase of the family and interacts with CCT
metabolism
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
CCT is an essential molecular chaperone system in the center of eukaryotic cell growth control and cell cycle regulation. Gene ontology analysis of the PfCCT interactome, overview
metabolism
-
CCT-actin system, overview. Interactions between CCT, actin and Plp2p in yeast: the actin map shows the CCT-binding sites, I, II and III and hinges, and the essential actin-binding D244 residue located in actin subdomain 4, which biochemically cross-links to the CCT8 subunit. Yeast actin (ACT1) binding to yeast CCT induces protease resistance in Cct4p and Cct8p. The PLP2 component shows its interactions with CCT subunits, CCT1, CCT4 and CCT8
-
physiological function
-
the enzyme can protect halophilic proteins against denaturation under conditions of cellular hyposaline stress
physiological function
chaperonins are ubiquitous molecular chaperones performing an ATP-dependent conformational change of the cavity that induces the folding of an unfolded protein that is captured in the cavity
physiological function
-
the enzymes TRiC/CCT are absolutely required for folding many essential proteins, including cytoskeletal proteins such as tubulin and actin, as well as cell cycle regulators such as CDC20 and CDH1. About 10% of cytosolic proteins interact with the eukaryotic chaperonin TRiC/CCT along their folding trajectory
physiological function
group II chaperonin proteins assist in the folding of nascent polypeptides and also refold unfolded proteins in an ATP-dependent manner. Chaperonin-mediated protein folding is dependent on the closure and opening of a built-in lid, which is controlled by the ATP hydrolysis cycle
physiological function
the CpkA C-terminal region plays a key role in cell growth at 60°C
physiological function
the group II chaperonin captures an unfolded protein while in its open conformation and then mediates the folding of the protein during ATP-driven conformational change cycle
physiological function
chaperonins are molecular machines that use ATP-driven cycles to assist misfolded substrate proteins to reach the native state. During the functional cycle, these machines adopt distinct nucleotide-dependent conformational states, which reflect large-scale allosteric changes in individual subunits. Archaeal and eukaryotic chaperonins undergo sequential subunit motions, analysis of the mode of action and mechanism. The thermosome double-ring structure has large contribution from higher-frequency modes
physiological function
chaperonins are ubiquitous chaperones that are required for correct protein folding, assembly, and degradation
physiological function
chaperonins are essential for protein folding in all domains of life. They stand out among ATP-dependent chaperones in that they form large 800-1000 kDa double-ring complexes with an internal chamber in each ring. Their basic function is to provide a nano-cage for the folding of single protein molecules to occur in isolation, unimpaired by aggregation
physiological function
chaperonins are essential for protein folding in all domains of life. They stand out among ATP-dependent chaperones in that they form large 800-1000 kDa double-ring complexes with an internal chamber in each ring. Their basic function is to provide a nano-cage for the folding of single protein molecules to occur in isolation, unimpaired by aggregation. Enzyme TRiC mediates protein folding by encapsulation and displays negative inter-ring cooperativity, favoring asymmetric complexes with one ring open and the other closed. The inner surface of the TRiC chamber is divided into two halves with opposite charge character. This charge asymmetry coincides with an asymmetry in ATP binding and hydrolysis: four adjacent subunits have high affinity for ATP and neutral or negative surface charge, while the other four subunits have low affinity for ATP and positive surface charge. Chamber closure and release of substrate protein can initiate asymmetrically and proceed in a sequential mechanism. TRiC also binds and masks polyQ-expanded fragments of the Huntington's disease protein, inhibiting their toxic aggregation
physiological function
chaperonins have elaborate allosteric mechanisms to regulate their functional cycle. Long-range negative cooperativity between the two rings ensures alternation of the folding chambers. No Positive intra-ring cooperativity in group II enzymes. Thermosomes use a non-specific, hydrophobic-based substrate recognition mechanism involving the helical protrusion, release of trapped substrate after closure of the chaperonin cavity
physiological function
chaperonins have elaborate allosteric mechanisms to regulate their functional cycle. Long-range negative cooperativity between the two rings ensures alternation of the folding chambers. No Positive intra-ring cooperativity in group II enzymes
physiological function
-
prefoldin is a molecular chaperone that can stabilize tentatively nascent polypeptide chains or non-native forms of mainly cytoskeletal proteins, which are subsequently delivered to group II chaperonin to accomplish their precise folding, active and passive effects of Pyrococcus furiosus prefoldin on the refolding reactions of Pyrococcus furiosus citrate synthase and Aequorea enhanced green fluorescence protein differ in the presence or absence of Pyrococcus furiosus chaperonin, PfuCPN
physiological function
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
chaperonins are essential for cell survival as they protect against proteotoxic stress that may lead to protein misfolding and aggregation. Chaperonin TRiC (T-complex protein-1 ring complex, also known as CCT) in the development and progression of cancer. Type II chaperonin TRiC/CCT contributes to oncogenesis. TRiC assists productive folding of substrate proteins by undergoing conformational changes that are ATP-dependent. Interaction of TRiC with p53 promotes the protein folding and activity of p53, a tumor suppressor protein that plays a critical role in preventing malignant cancer cell development. p53 primarily functions as a transcription factor that modulates the expression of a variety of genes involved in cellular responses such as cell-cycle arrest and apoptosis. Contribution of TRiC to mutant p53-mediated oncogenesis is not as straightforward as it is for STAT3. TRiC plays a critical role in the regulation of cell cycle progression and modulates cell cycle regulatory proteins
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
chaperonins are essential for cell survival as they protect against proteotoxic stress that may lead to protein misfolding and aggregation. Chaperonin TRiC (T-complex protein-1 ring complex, also known as CCT) is involved in the development and progression of cancer mediated through its critical interactions with oncogenic clients, it modulates growth deregulation, apoptosis, and genome instability in cancer cells. Type II chaperonin TRiC/CCT contributes to oncogenesis. TRiC assists productive folding of substrate proteins by undergoing conformational changes that are ATP-dependent. Interaction of TRiC with p53 promotes the protein folding and activity of p53, a tumor suppressor protein that plays a critical role in preventing malignant cancer cell development. p53 primarily functions as a transcription factor that modulates the expression of a variety of genes involved in cellular responses such as cell-cycle arrest and apoptosis. Contribution of TRiC to mutant p53-mediated oncogenesis is not as straightforward as it is for STAT3. TRiC contributes to STAT protein folding and function, STAT3 requires TRiC for folding and proper functioning. TRiC plays a critical role in the regulation of cell cycle progression and modulates cell cycle regulatory proteins. HSP70 and TRiC appear to function sequentially in the Von Hippel-Lindau protein (VHL) folding pathway, with loss of HSP70 function blocking association with TRiC and loss of TRiC function having no effect on HSP70 association. TRiC subunits, CCT2 and CCT1, are essential for survival and proliferation of breast cancer. Chaperonin TRiC works as an assembly station for the tumor suppressor protein, VHL (Von Hippel-Lindau), mechanism, overview. TRiC chaperonin contributes to carcinogenesis through its contribution to STAT3 signaling
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
chaperonin TRiC/CCT modulates the folding and activity of leukemogenic fusion oncoprotein AML1-ETO. AML1-ETO is the most common fusion oncoprotein causing acute myeloid leukemia (AML), a disease with a 5-year survival rate of only 24%. AML1-ETO functions as a rogue transcription factor, altering the expression of genes critical for myeloid cell development and differentiation. The biosynthesis and folding of the AML1-ETO protein is facilitated by interaction with the essential eukaryotic chaperonin TRiC (or CCT)
physiological function
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
chaperonin TRiC/CCT modulates the folding and activity of leukemogenic fusion oncoprotein AML1-ETO. AML1-ETO is the most common fusion oncoprotein causing acute myeloid leukemia (AML), a disease with a 5-year survival rate of only 24%. AML1-ETO functions as a rogue transcription factor, altering the expression of genes critical for myeloid cell development and differentiation. The biosynthesis and folding of the AML1-ETO protein is facilitated by interaction with the essential eukaryotic chaperonin TRiC (or CCT)
physiological function
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
the chaperonin-containing t-complex polypeptide 1 (CCT or TRiC) assists protein folding in an ATP-dependent manner. CCT/TRiC has been found to mediate the folding of beta-actin, alpha- and beta-tubulin, and several hundred other proteins in addition to several clinically important proteins such as p53 and the oncoprotein AML1-ETO
physiological function
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
TRiC directly interacts with heat shock factor protein 1 (HSF1) and represses its transcriptional activity
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the eukaryotic TRiC chaperonin controls reovirus replication through outer-capsid folding, TRiC (also called CCT) is a cellular factor required for late events in the replication of mammalian reovirus. TRiC is essential for reovirus replication. TRiC forms a complex with the reovirus sigma3 outer-capsid protein and folds sigma3 into its into a native, assembly-competent conformation. TRiC renders sigma3 into a conformation that can assemble onto mature particles, which is a critical step in viral assembly, determination of a dynamic pathway for the efficient folding of viral capsid components mediated by the TRiC chaperonin, overview. Six of the eight subunits of the TRiC chaperonin (CCT1, CCT2, CCT3, CCT4, CCT5, and CCT8) are implicated in viral replication, siRNA mutational analysis, overview
physiological function
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
chaperonin containing TCP-1 (CCT) is a complex that assists protein folding and function. The CCT complex is required for organ growth by interacting with the TOR pathway in Drosophila melanogaster. The CCT complex regulates organ growth by directly interacting with the TOR signaling pathway, interaction with TOR signaling components including TOR, Rheb, and S6K. Analysis of the genetic interaction between CCT complex and growth signaling pathways, overview
physiological function
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
chaperonin TCP-1 ring complex (TRiC) supports proper folding of numerous proteins including cell cycle regulators and mediates protein quality control. TRiC/CCT supports mitotic exit and entry into endocycle in Drosophila melanogaster. The evolutionarily conserved chaperonin TRiC is a regulator of the mitotic-to-endocycle switch (MES), which is critical for the prothoracic gland (PG) to upregulate biosynthesis of the steroid hormone ecdysone. TRiC supports proper MES and endocycle progression by regulating Fzr folding. TRiC-mediated protein quality control is proposed to be a conserved mechanism supporting MES and endocycling, as well as subsequent terminal differentiation. TRiC is required for ecdysone biosynthesis in the PG to induce the larval-to-pupal transition. TRiC downregulates CycA by regulating Fzr nuclear translocation to promote MES and endocycling
physiological function
-
the eukaryotic group II chaperonin, the chaperonin-containing t-complex polypeptide 1 (CCT), plays an important role in cytosolic proteostasis. About 10% of cytosolic proteins interact with CCT during their folding process. Expression of CCT is not induced by stress conditions, but it seems to be required for folding newly synthesized polypeptides. Despite its substrate specificity, CCT is absolutely required for folding many essential proteins, including cytoskeletal proteins such as tubulin and actin, as well as cell cycle regulators, such as CDC20 and CDH1
physiological function
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
chaperonins are large, multimeric, barrel-shaped proteins, which assist in the folding and prevent aggregation of non-native proteins. The protein MreB structure is rearranged by a binding-induced expansion mechanism in TRiC, GroEL and GroES. These results are quantitatively comparable to the structural rearrangements found during the interaction of beta-actin with GroEL and TRiC. The chaperonin-bound MreB is also significantly compacted after addition of AMP-PNP for both the GroEL/ES and TRiC systems. Most importantly, GroES may act as an unfoldase by inducing a dramatic initial expansion of MreB (even more than for GroEL) implicating a role for MreB folding, suggesting a delivery mechanism for GroES to GroEL in prokaryotes
physiological function
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
the TCP-1 ring complex (TRiC) is a multi-subunit group II chaperonin that assists nascent or misfolded proteins to attain their native conformation in an ATP-dependent manner. Zebrafish chaperonin TRiC has a specific role in the biogenesis of skeletal muscle alpha-actin during sarcomere assembly in myofibers. TRiC only enhances the folding of skeletal alpha-actin at the sarcomeric Z-disk. ATP binding by subunit CCT5 is required for folding of alpha-actin, but probably not tubulin. TRiC function is required for myopathic actin to form rods in nemaline myopathy. TRiC causes aggregation of myopathic alpha-actin mutant variants in nemaline myopathy. ATP Binding by CCT5 is specific for skeletal muscle alpha-actin but not tubulin processing. TRiC function is required for nemaline rod formation resulting from the expression of disease-causing skeletal muscle alpha-actin variants
physiological function
chaperonins (CPNs) are ubiquitous, double ring-shaped molecular chaperones that capture unfolded proteins in their cavities and assist in protein folding in an ATP-dependent manner. Prefoldin (PFD) captures an unfolded protein substrate and transfers it to a group II chaperonin (CPN). The transfer of a substrate from PFD to CPN involves a direct interaction, PFD interacts with the apical domain of CPN, analysis of protein-folding mechanism of PFD and CPN using the PFD-CPN systems of the hyperthermophilic archaea, overview
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
subunits CCT2 and CCT7 interact with tumour suppressors p53 and VHL, respectively. The enzyme is involved in breast cancer signaling via STAT3, and in apoptosis via CCT2 and PDC5, or BAG3. Subunit CCT8 interacts with AML-ETO in leukemia. Subunits CCT2, 3, and 8 are involved in mRNA overexpression in cancer cells. Subunit CCT7 is involved in fibroblast motility. Subunits CCT2, 5, and 7 are required for autophagy. The CCT complex is involved in disassembly of the mitotic checkpoint, artherosclerosis, and cell survival, and in several other cellular processes, overview
physiological function
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
subunits CCT1, CCT3, CCT4 and CCT8 are all essential for spermatogenesis. The CCT3/gamma domain in FAB1p is involved in autophagy
physiological function
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
subunit CCT8 and the CCT complex are involved in Ras signalling and morphogenesis, and in the polarisome and cell polarity, respectively
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the essential mammalian cytosolic chaperonin TRiC (T-complex polypeptide-1 ring complex, also known as CCT or chaperonin containing TCP1) is an ATPase with an intricate architecture, which allows it to fold many essential proteins. TRiC substrates include cell cycle regulators, signaling proteins, and cytoskeletal components. TRiC has been suggested to play a critical role in cancer cell development by modulating the folding and activity of client proteins involved in oncogenesis, such as the tumor suppressor proteins Von Hippel-Lindau (VHL) and p53, as well as the oncogenic protein STAT3 and AML1-ETO. AML1-ETO is the translational product of a chimeric gene created by the stable chromosome translocation. It causes acute myeloid leukemia (AML) by dysregulating the expression of genes critical for myeloid cell development and differentiation and has been reported to bind multiple subunits of the mammalian cytosolic chaperonin TRiC (or CCT), primarily through its DNA binding domain (AML1-175). Through these interactions, TRiC plays an important role in the synthesis, folding, and activity of AML1-ETO. The structure reveals that AML1-175 associates directly with a specific subset of TRiC subunits in the open conformation. The mammalian cytosolic chaperonin TRiC (or CCT) modulates the synthesis, folding and activity of AML1-ETO by direct association, primarily through its DNA-binding domain (AML1-175), and that HSP70 promotes this interaction. AML1-ETO relies on the molecular chaperone network to fold and function properly
physiological function
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
the enzyme is involved in invasion and lifespan extension
physiological function
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
subunit CCT5 is involved in thin filament assembly at the sarcomere Z-disk. Three BBS proteins which have homology to chaperonins, BBS6, BBS10 and BBS12, and a sub-complex of CCT proteins (CCT1, 2, 3, 4, 5 and 8) mediate the association of two beta-propeller domain-containing proteins, BBS7 and BBS2, during the assembly process of the BBSome. BBS6, -10 and -12 are vertebrate-specific proteins and it may be an evolutionary connection that one of the two absent CCT subunits in the BBS-CCT complex, CCT6, has a vertebrate-specific isoform, CCT6B, which is abundant in testis CCT. CCT6 self-interacts across the CCT rings which probably permits isoform interchange, and therefore, it is possible that one of the BBS subunits has hijacked this mechanism and is able to slot into the CCT6 position in the CCT ring system
physiological function
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
the enzyme complex CCT is involved in stem cell identity and protein translocation
physiological function
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
CCT is a key modulator of echinocandin susceptibility
physiological function
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
subunit CCT1 is involved in fragile X-linked and cell identity, subunit CCT5 is required for autophagy
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
direct interactions between two chaperonins allow them to feed folding substrates bi-directionally between active sites, preventing aggregation and promoting proteostasis. The essential ring-shaped chaperonin TRiC/CCT cooperates with the chaperone prefoldin/GIMc (PFD). These hetero-oligomeric chaperones associate in a defined architecture, through a conserved interface of electrostatic contacts that serves as a pivot point for a TRiC-PFD conformational cycle. PFD pivots around a conserved electrostatic interface with TRiC/CCT PFD acts on TRiC/CCT-substrate complex to enhance the rate of the folding reaction, overview. The suprachaperone assembly formed by PFD and TRiC is essential to prevent toxic conformations and ensure effective cellular proteostasis
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
The hetero-oligomeric chaperonin of eukarya, TRiC, is required to fold the cytoskeletal protein actin. The eukaryotic chaperone complex TRiC, but not the simpler bacterial chaperonin system, GroEL/GroES, is able to induce the proper folding of actin. Actin fails to fold spontaneously, strictly requiring TRiC chaperonin for folding. Actin binding to TRiC specifies a unique topology for productive folding. ATP binding induces an asymmetric TRiC intermediate and selective actin release. Stepwise folding on and inside TRiC allows actin to access the native state
physiological function
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
the chaperonin containing t-complex polypeptide-1 which is also known as TRiC plays a central role in cellular homeostasis by facilitating the folding of approximately 10% or more of newly synthesized proteins which include tubulins, actins, luciferin, Von Hippel-Lindau disease tumor suppressor (VHL), histone deacetylase 3, and other client proteins. Enzyme GaTRiC is important in cell regulation
physiological function
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
the malaria parasite exports numerous proteins into its host red blood cell (RBC). Proteins are first routed through the secretory system, into the parasitophorous vacuole (PV), a membranous compartment enclosing the parasite. Proteins are then translocated across the PV membrane in a process requiring ATP and unfolding. Once in the RBC compartment the exported proteins are then refolded and further trafficked to their final localizations. Chaperones are important in the unfolding and refolding processes. The parasite TRiC chaperonin complex is exported, and is involved in trafficking of exported effectors. Essential role for PfTRiC within the parasite compartment. Subunit PfTRiC-theta is essential for asexual parasite growth
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the malaria parasite exports numerous proteins into its host red blood cell (RBC). Proteins are first routed through the secretory system, into the parasitophorous vacuole (PV), a membranous compartment enclosing the parasite. Proteins are then translocated across the PV membrane in a process requiring ATP and unfolding. Once in the RBC compartment the exported proteins are then refolded and further trafficked to their final localizations. Chaperones are important in the unfolding and refolding processes. The parasite TRiC chaperonin complex is exported, and is involved in trafficking of exported effectors. Essential role for PfTRiC within the parasite compartment
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
TRiC is a multi-protein chaperone complex that functions to assist polypeptides in achieving a functional three-dimensional configuration. It has an essential role in folding the highly abundant cytoskeletal proteins actin and tubulin The TCP1 and CCT2 genes both encode for components of a multi-protein chaperone complex in the cell known as the TCP1 containing ring complex (TRiC). The TRiC subunits TCP1 and CCT2, and potentially the entire TRiC complex, play a role in breast cancer. TCP1 and CCT2 are recurrently altered in breast cancer and necessary for growth/survival of breast cancer cells in vitro, they are determinants of overall survival in breast cancer patients. Expression of TCP1 is regulated by driver oncogene activation of PI3K signaling in breast cancer. Role for CCT2 in cell cycle progression. The TCP1 subunit of TRiC is both regulated by FGFR2 and necessary for cell growth in SUM-52 cells. the TCP1 subunit of TRiC is regulated by FGFR2, necessary for proliferation of breast cancer cells and associated with poor overall survival of breast cancer patients
physiological function
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
eukaryotic cytoplasmic chaperonins are key elements responsible for this proper folding of proteins, including that of cytoskeletal components. Protein folding is mediated in the eukaryotic cytosol by the TCP-1 ring large multi-subunit complex (TRiC), also called CCT. TRiC/CCT chaperonins are essential for maintaining myofibril organization, cardiac physiological rhythm, and lifespan. TRiC/CCT chaperonins are essential for actin and myosin containing myofibril integrity. Both the orchestration of protein folding and circadian rhythms mediated by CCT chaperonin are critical for maintaining heart contractility
physiological function
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
the cytosolic T-complex protein-1 ring complex (TRiC), also referred as chaperonin containing TCP-1(CCT), comprising eight different subunits stacked in double toroidal rings, binds to around 10% of newly synthesized polypeptides and facilitates their folding in ATP dependent manner. Subunit LdTCP1gamma forms biologically active homo-oligomeric complex and plays role in protein folding and parasite survival. The dimeric and tetrameric assembly of the epsilon subunit shows chaperonin activity, ATPase, and luciferase refolding activity
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the eukaryotic chaperonin containing tailless complex polypeptide 1 ring complex (CCT, also known as TCP-1 ring complex, TRiC/CCT) participates in the folding of 5-10% of the cellular proteome and is involved in the life cycle of several viruses, including dengue, Zika, and influenza viruses. The nucleoprotein (NP) of the mammarenavirus lymphocytic choriomeningitis virus (LCMV) is a substrate of the human TRiC/CCT complex. The TRiC/CCT complex is required for the production of NP-containing virus-like particles (VLPs), and the activity of the virus ribonucleoprotein (vRNP) responsible for directing replication and transcription of the viral genome. LCMV NP binds to the different components of the chaperonin TRiC/CCT complex. Analysis of the interaction between LCMV NP and components of the TRiC/CCT complex using HA-tagged LCMV nucleoprotein and FLAG-tagged human TCP1, or CCT2- to CCT8-expressing plasmids expressed in HEK-293T cells, overview
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
accurate folding of proteins in living cells often requires the cooperative support of molecular chaperones. Eukaryotic group II chaperonin Tailless complex polypeptide 1-ring complex (TRiC) accomplishes this task by providing a folding chamber for the substrate that is regulated by an adenosine triphosphate (ATP) hydrolysis-dependent cycle. Once delivered to and recognized by TRiC, the nascent substrate enters the folding chamber and undergoes folding and release in a stepwise manner. During the process, TRiC subunits and co-chaperones such as prefoldin and phosducin-like proteins interact with the substrate to assist the overall folding process in a substrate-specific manner. Coevolution between the components is supposed to consult the binding specificity and ultimately expand the substrate repertoire assisted by the chaperone network
physiological function
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
accurate folding of proteins in living cells often requires the cooperative support of molecular chaperones. Eukaryotic group II chaperonin Tailless complex polypeptide 1-ring complex (TRiC) accomplishes this task by providing a folding chamber for the substrate that is regulated by an adenosine triphosphate (ATP) hydrolysis-dependent cycle. Once delivered to and recognized by TRiC, the nascent substrate enters the folding chamber and undergoes folding and release in a stepwise manner. During the process, TRiC subunits and co-chaperones such as prefoldin and phosducin-like proteins interact with the substrate to assist the overall folding process in a substrate-specific manner. Coevolution between the components is supposed to consult the binding specificity and ultimately expand the substrate repertoire assisted by the chaperone network
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
TRiC-mediated protein folding depends on an ATP-driven conformational cycle,which regulates the opening and closing of a built-in lid over the central chamber of each ring. In the apo-state, the lid is open and substrates bind to the apical domains of specific CCT subunits. ATP hydrolysis leads to lid formation and substrate encapsulation in the closed central chamber, where folding occurs. TRiC functions in cooperation with many cochaperones, including prefoldin (PFD) and phosducin-like proteins. Structure-function mechanism, detailed overview
physiological function
-
chaperonins are homo- or hetero-oligomeric complexes that use ATP binding and hydrolysis to facilitate protein folding. Chaperonins bind non-native polypeptides in their central cavity and consume ATP to mediate correct polypeptide folding. ATP hydrolysis exhibits both positive and negative cooperativity
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
role of the chaperonin CCT in mTOR complex assembly, binding structures and interaction analysis, detailed overview. Rapamycin (mTOR) kinase forms two multi-protein signaling complexes, mTORC1 and mTORC2, which are master regulators of cell growth, metabolism, survival and autophagy. The eukaryotic chaperonin CCT plays a key role in mTORC assembly and signaling by folding both subunits mLST8 and Raptor, beta-propeller proteins that stabilize the mTOR kinase and recruit substrates, respectively. Robust interaction between mLST8 or human Raptor and CCT. Co-chaperone PhLP1 does not assist in mTORC assembly
physiological function
F6T521; F6PJP5; G7MDZ6; A0A5F7ZBU8; A0A1D5Q8I4; I0FKJ8; A0A1D5RDC8; A0A5F7Z7P5
the tailless complex polypeptide I ring complex (TRiC) is a cellular chaperonin responsible for folding at least 10% of the cytosolic proteins. The eukaryotic cytosolic ATP-dependent chaperonin TRiC is critical for rotavirus (RV) replication by controlling dsRNA genome segment synthesis, particularly negative-sense single-stranded RNA. TRiC associates with viral VP2, the cofactor involved in RNA replication, and NSP5, but not with VP1
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
while most small proteins fold rapidly on their own, many larger proteins with complex topologies are prone to misfolding, becoming trapped in alternate states by an insurmountable free energy barrier. Cytosolic chaperonin CCT uses its distinctive subunit arrangement to fold structurally unrelated substrates (proteins folded by CCT), CCT-substrate interaction structures, binding sites and mechanisms, overview. In addition to protein folding, CCT contributes to the assembly of protein complexes by first folding one or more subunits of the client complex and then providing a platform on which the complex can assemble or by releasing the subunit as it associates with its binding partners. Substrate folding trajectories are also mediated by asymmetry of charge distribution within the CCT chamber itself
physiological function
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
while most small proteins fold rapidly on their own, many larger proteins with complex topologies are prone to misfolding, becoming trapped in alternate states by an insurmountable free energy barrier. Cytosolic chaperonin CCT uses its distinctive subunit arrangement to fold structurally unrelated substrates (proteins folded by CCT), CCT-substrate interaction structures, binding sites and mechanisms, overview
physiological function
chaperonin containing TCP1 subunit 6A (CCT6A) participates in intracellular protein folding and aggregation and is involved in cancer pathogenesis and stemness. CCT6A is an oncogene that participates in the initiation of various cancers, it may activate Notch and Wnt pathways to facilitate the malignant behaviors and cancer stemness in oral squamous cell carcinoma (OSCC). The Wnt and Notch pathways are involved in the CCT6A-effect on SCC-15 cell functions. CCT6A positively regulates the Wnt and Notch pathways in SCC-15 and HSC-3 cells. CCT6A may promote OSCC malignant behavior and stemness by activating the Wnt and Notch pathways
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the ATP-dependent ring-shaped chaperonin TRiC/CCT is essential for cellular proteostasis, it facilitates folding of a subset of proteins comprising about 10% of the eukaryotic proteome. The proteins that require TRiC for folding, many of them essential for viability, are distinguished by their aggregation propensity and topological complexity. In vivo, TRiC functions in cooperation with upstream chaperones, including Hsp70 and prefoldin (PFD, also called GIMc). Prefoldin binds directly to TRiC through an electrostatic pivot, suggesting a direct mechanism of substrate transfer
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
chaperonins depend on adenosine triphosphate (ATP) binding and hydrolysis to bind and fold non-native proteins within their enclosed central chamber. Besides modulating proteostasis as a chaperonin, TRiC/CCT regulates cell cycle, transcription and translation initiation, immortality, epigenetic changes, T-cell immunity, autophagy and signal transduction. TRiC/CCT is required for the folding of many essential proteins. TRiC/CCT either interacts directly with substrate proteins or utilises cofactors such as prefoldin and HSP70 for substrate delivery. Protein interactome and biological functions of TRIC/CCT, detailed overview. The multifaceted functions of TRiC/CCT extend across diverse biological processes, making it a critical player in maintaining proteostasis and cellular functionality
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the chaperonin-containing TCP-1 (CCT) complex is a cellular machine that assists in protein folding and function. The CCT complex interacts specifically with A3A, a APOBEC3 cytidine deaminase, and APOBEC3A interacts with all subunits of the CCT chaperonin complex, detailed interaction analysis, overview. The CCT complex interacts with APOBEC3A in multiple cell types
physiological function
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
WDTC1 is a WD40-containing protein that functions as an anti-obesity factor, it inhibits adipogenesis by working as an adaptor of the CUL4-DDB1 E3 ligase complex. TRiC/CCT functions essentially as a chaperone to facilitate the protein folding of WDTC1 and proper function in adipogenesis. TRiC/CCT is required for the stability of WDTC1
physiological function
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
WDTC1 is a WD40-containing protein that functions as an anti-obesity factor, it inhibits adipogenesis by working as an adaptor of the CUL4-DDB1 E3 ligase complex. TRiC/CCT functions essentially as a chaperone to facilitate the protein folding of WDTC1 and proper function in adipogenesis. TRiC/CCT is required for the stability of WDTC1
physiological function
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
the multi-subunit chaperonin containing TCP-1 (CCT) is an ATPase and an essential molecular chaperone that functions in the folding of key cellular proteins. Upon binding and hydrolysis of ATP, CCT encapsulates and folds non-native proteins. Primary clients are the ubiquitous cytoskeletal proteins, actin and tubulin. CCT also interacts with other nascent proteins, especially the WD40 propeller proteins, and also assists in the assembly of several protein complexes. CCT is essential for asexual development in Plasmodium falciparum, the complex has less involvement with proteins involved in pathogenesis and host-cell interaction
physiological function
-
chaperonin TCP-1 ring complex (TRiC) supports proper folding of numerous proteins including cell cycle regulators and mediates protein quality control. TRiC/CCT supports mitotic exit and entry into endocycle in Drosophila melanogaster. The evolutionarily conserved chaperonin TRiC is a regulator of the mitotic-to-endocycle switch (MES), which is critical for the prothoracic gland (PG) to upregulate biosynthesis of the steroid hormone ecdysone. TRiC supports proper MES and endocycle progression by regulating Fzr folding. TRiC-mediated protein quality control is proposed to be a conserved mechanism supporting MES and endocycling, as well as subsequent terminal differentiation. TRiC is required for ecdysone biosynthesis in the PG to induce the larval-to-pupal transition. TRiC downregulates CycA by regulating Fzr nuclear translocation to promote MES and endocycling
-
physiological function
-
the cytosolic T-complex protein-1 ring complex (TRiC), also referred as chaperonin containing TCP-1(CCT), comprising eight different subunits stacked in double toroidal rings, binds to around 10% of newly synthesized polypeptides and facilitates their folding in ATP dependent manner. Subunit LdTCP1gamma forms biologically active homo-oligomeric complex and plays role in protein folding and parasite survival. The dimeric and tetrameric assembly of the epsilon subunit shows chaperonin activity, ATPase, and luciferase refolding activity
-
physiological function
-
chaperonins are ubiquitous molecular chaperones performing an ATP-dependent conformational change of the cavity that induces the folding of an unfolded protein that is captured in the cavity
-
physiological function
-
group II chaperonin proteins assist in the folding of nascent polypeptides and also refold unfolded proteins in an ATP-dependent manner. Chaperonin-mediated protein folding is dependent on the closure and opening of a built-in lid, which is controlled by the ATP hydrolysis cycle
-
physiological function
-
the group II chaperonin captures an unfolded protein while in its open conformation and then mediates the folding of the protein during ATP-driven conformational change cycle
-
physiological function
-
chaperonins are essential for protein folding in all domains of life. They stand out among ATP-dependent chaperones in that they form large 800-1000 kDa double-ring complexes with an internal chamber in each ring. Their basic function is to provide a nano-cage for the folding of single protein molecules to occur in isolation, unimpaired by aggregation. Enzyme TRiC mediates protein folding by encapsulation and displays negative inter-ring cooperativity, favoring asymmetric complexes with one ring open and the other closed. The inner surface of the TRiC chamber is divided into two halves with opposite charge character. This charge asymmetry coincides with an asymmetry in ATP binding and hydrolysis: four adjacent subunits have high affinity for ATP and neutral or negative surface charge, while the other four subunits have low affinity for ATP and positive surface charge. Chamber closure and release of substrate protein can initiate asymmetrically and proceed in a sequential mechanism. TRiC also binds and masks polyQ-expanded fragments of the Huntington's disease protein, inhibiting their toxic aggregation
-
physiological function
-
the chaperonin-containing t-complex polypeptide 1 (CCT or TRiC) assists protein folding in an ATP-dependent manner. CCT/TRiC has been found to mediate the folding of beta-actin, alpha- and beta-tubulin, and several hundred other proteins in addition to several clinically important proteins such as p53 and the oncoprotein AML1-ETO
-
physiological function
-
subunit CCT8 and the CCT complex are involved in Ras signalling and morphogenesis, and in the polarisome and cell polarity, respectively
-
physiological function
-
accurate folding of proteins in living cells often requires the cooperative support of molecular chaperones. Eukaryotic group II chaperonin Tailless complex polypeptide 1-ring complex (TRiC) accomplishes this task by providing a folding chamber for the substrate that is regulated by an adenosine triphosphate (ATP) hydrolysis-dependent cycle. Once delivered to and recognized by TRiC, the nascent substrate enters the folding chamber and undergoes folding and release in a stepwise manner. During the process, TRiC subunits and co-chaperones such as prefoldin and phosducin-like proteins interact with the substrate to assist the overall folding process in a substrate-specific manner. Coevolution between the components is supposed to consult the binding specificity and ultimately expand the substrate repertoire assisted by the chaperone network
-
physiological function
-
while most small proteins fold rapidly on their own, many larger proteins with complex topologies are prone to misfolding, becoming trapped in alternate states by an insurmountable free energy barrier. Cytosolic chaperonin CCT uses its distinctive subunit arrangement to fold structurally unrelated substrates (proteins folded by CCT), CCT-substrate interaction structures, binding sites and mechanisms, overview
-
physiological function
-
CCT is a key modulator of echinocandin susceptibility
-
physiological function
-
chaperonins are molecular machines that use ATP-driven cycles to assist misfolded substrate proteins to reach the native state. During the functional cycle, these machines adopt distinct nucleotide-dependent conformational states, which reflect large-scale allosteric changes in individual subunits. Archaeal and eukaryotic chaperonins undergo sequential subunit motions, analysis of the mode of action and mechanism. The thermosome double-ring structure has large contribution from higher-frequency modes
-
physiological function
-
chaperonins have elaborate allosteric mechanisms to regulate their functional cycle. Long-range negative cooperativity between the two rings ensures alternation of the folding chambers. No Positive intra-ring cooperativity in group II enzymes. Thermosomes use a non-specific, hydrophobic-based substrate recognition mechanism involving the helical protrusion, release of trapped substrate after closure of the chaperonin cavity
-
physiological function
-
chaperonins are ubiquitous molecular chaperones performing an ATP-dependent conformational change of the cavity that induces the folding of an unfolded protein that is captured in the cavity
-
physiological function
Leishmania donovani MHOM/IN/80
-
the cytosolic T-complex protein-1 ring complex (TRiC), also referred as chaperonin containing TCP-1(CCT), comprising eight different subunits stacked in double toroidal rings, binds to around 10% of newly synthesized polypeptides and facilitates their folding in ATP dependent manner. Subunit LdTCP1gamma forms biologically active homo-oligomeric complex and plays role in protein folding and parasite survival. The dimeric and tetrameric assembly of the epsilon subunit shows chaperonin activity, ATPase, and luciferase refolding activity
-
additional information
chaperonins are ubiquitous molecular chaperones with the subunit molecular mass of 60 kDa. They exist as double-ring oligomers with central cavities. An ATP-dependent conformational change of the cavity induces the folding of an unfolded protein that is captured in the cavity. Inter-ring communication is dispensable in the reaction cycle of group II chaperonins. Group II chaperonins do not require a co-chaperonin but have a built-in lid that is composed of a helical protrusion in the apical domain. The built-in lid seals off the central cavity and induces a conformational change to assist the folding of the trapped substrate, molecular mechanism analysis. Structure modeling of wild-type and mutant enzyme oligomers using structure of Thermococcus sp. JCM 11816, PDB ID 1Q2V, overview
additional information
chaperonins are ubiquitous molecular chaperones with the subunit molecular mass of 60 kDa. They exist as double-ring oligomers with central cavities. An ATP-dependent conformational change of the cavity induces the folding of an unfolded protein that is captured in the cavity. Inter-ring communication is dispensable in the reaction cycle of group II chaperonins. Group II chaperonins do not require a co-chaperonin but have a built-in lid that is composed of a helical protrusion in the apical domain. The built-in lid seals off the central cavity and induces a conformational change to assist the folding of the trapped substrate, molecular mechanism analysis. Structure modeling of wild-type and mutant enzyme oligomers using structure of Thermococcus sp. JCM 11816, PDB ID 1Q2V, overview
additional information
-
enzyme structure and architecture comparisons and modeling, structure-function analysis of group II chaperonins, ATP-driven conformational cycle of the group II chaperonin, overview
additional information
-
enzyme structure and architecture comparisons and modeling, structure-function analysis of group II chaperonins, ATP-driven conformational cycle of the group II chaperonin, overview
additional information
-
enzyme structure and architecture comparisons and modeling, structure-function analysis of group II chaperonins, ATP-driven conformational cycle of the group II chaperonin, overview
additional information
determination of ATP-dependent dynamics of a group II chaperonin at the single-molecule level with highly accurate rotational axes views by UV light-triggered diffracted X-ray tracking, using caged-ATP and stopped-flow fluorometry. The closed ring twists counterclockwise and the twisted ring reverted to the original open-state with a clockwise motion, the biphasic lid-closure process occurs with unsynchronized closure and a synchronized counterclockwise twisting motion
additional information
determination of ATP-dependent dynamics of a group II chaperonin at the single-molecule level with highly accurate rotational axes views by UV light-triggered diffracted X-ray tracking, using caged-ATP and stopped-flow fluorometry. The closed ring twists counterclockwise and the twisted ring reverted to the original open-state with a clockwise motion, the biphasic lid-closure process occurs with unsynchronized closure and a synchronized counterclockwise twisting motion
additional information
reaction cycle model for group II chaperonins, ATP-binding, stopped-flow fluorometry and stopped-flow small-angle X-ray scattering, overview
additional information
reaction cycle model for group II chaperonins, ATP-binding, stopped-flow fluorometry and stopped-flow small-angle X-ray scattering, overview
additional information
three-dimensional structures of nucleotide states of thermosome and allosteric communications within the archaeal chaperonin thermosome, open and closed states and transitional conformation changes, computational analysis, overview
additional information
three-dimensional structures of nucleotide states of thermosome and allosteric communications within the archaeal chaperonin thermosome, open and closed states and transitional conformation changes, computational analysis, overview
additional information
group II chaperonins exist as an 8- or 9-membered rotationally symmetrical double-ring in a toridal structure composed of homologous subunits of about 60 kDa. Each ring has a large central cavity in which a non-native protein can undergo productive folding in an ATP-dependent manner. A unique structural feature, termed the helical protrusion, acts as a built-in lid to seal off the central cavity of group II chaperonins during folding. Opening and closing of the folding chamber is controlled by a conformational cycle driven by ATP binding and hydrolysis. All chaperonins share a similar subunit architecture consisting of three distinct domains as follows: an ATP-binding equatorial domain, a distal apical domain harboring the polypeptide-binding sites, and an intermediate hinge domain
additional information
group II chaperonins exist as an 8- or 9-membered rotationally symmetrical double-ring in a toridal structure composed of homologous subunits of about 60 kDa. Each ring has a large central cavity in which a non-native protein can undergo productive folding in an ATP-dependent manner. A unique structural feature, termed the helical protrusion, acts as a built-in lid to seal off the central cavity of group II chaperonins during folding. Opening and closing of the folding chamber is controlled by a conformational cycle driven by ATP binding and hydrolysis. All chaperonins share a similar subunit architecture consisting of three distinct domains as follows: an ATP-binding equatorial domain, a distal apical domain harboring the polypeptide-binding sites, and an intermediate hinge domain
additional information
group II chaperonins exist as an 8- or 9-membered rotationally symmetrical double-ring in a toridal structure composed of homologous subunits of about 60 kDa. Each ring has a large central cavity in which a non-native protein can undergo productive folding in an ATP-dependent manner. A unique structural feature, termed the helical protrusion, acts as a built-in lid to seal off the central cavity of group II chaperonins during folding. Opening and closing of the folding chamber is controlled by a conformational cycle driven by ATP binding and hydrolysis. All chaperonins share a similar subunit architecture consisting of three distinct domains as follows: an ATP-binding equatorial domain, a distal apical domain harboring the polypeptide-binding sites, and an intermediate hinge domain
additional information
group II chaperonins generally contain eight subunits per ring and have a tendency to heterooligomer formation. TRiC contains eight paralogous subunits per ring assembled in a defined order
additional information
group II chaperonins generally contain eight subunits per ring and have a tendency to heterooligomer formation. TRiC contains eight paralogous subunits per ring assembled in a defined order
additional information
-
ATP hydrolysis enhances the intra-ring TRiC subunit interactions, asymmetrically closed conformation of TRiC and expansion of the folding chambers in the ATP hydrolysis transition state, and chamber closing mechanisms of TRiC, structure modeling, overview. Mechanism of TRiC negative inter-ring cooperativity. The TRiC lid remains open in three states of the cycle: ATP bound, ADP bound, and nucleotide free
additional information
mechanisms and the structure-function relationships in the complex protein systems, structural dynamics, allostery, and associated conformational rearrangements, overview. Group II chaperonins cycle between an open, substrate-receptive conformation and a closed, substrate-trapping conformation, structure modeling, detailed overview
additional information
mechanisms and the structure-function relationships in the complex protein systems, structural dynamics, allostery, and associated conformational rearrangements, overview. Group II chaperonins cycle between an open, substrate-receptive conformation and a closed, substrate-trapping conformation, structure modeling, detailed overview
additional information
group II chaperonins cycle between an open, substrate-receptive conformation and a closed, substrate-trapping conformation, structure modeling, detailed overview
additional information
group II chaperonins cycle between an open, substrate-receptive conformation and a closed, substrate-trapping conformation, structure modeling, detailed overview
additional information
group II chaperonins cycle between an open, substrate-receptive conformation and a closed, substrate-trapping conformation CCT (chaperonin containing TCP1) or TRiC (TCP1 ring complex) is composed of eight distinct subunits (CCTalpha-1, CCTbeta-2, CCTgamma-3, CCTdelta-4, CCTepsilon-5, CCTzeta-6, CCTeta-7 and CCTtheta-8) organized in a unique intra- and inter-ring arrangement, structure modeling, detailed overview. The substrate-binding region in each of the subunits bears charged and hydrophilic residues in some subunits, whereas other subunits have hydrophobic residues
additional information
possesses two chaperonins, cold-inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high temperatures, respectively. Clear correlation between the CpkA-type chaperonin gene copy number and growth temperature
additional information
possesses two chaperonins, cold-inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high temperatures, respectively. Clear correlation between the CpkA-type chaperonin gene copy number and growth temperature
additional information
possesses two chaperonins, cold-inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high temperatures, respectively
additional information
possesses two chaperonins, cold-inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high temperatures, respectively
additional information
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
large conformational changes occur upon nucleotide binding and hydrolysis. The conformational cycling begins with the binding of ATP and a transition of the complex to the closed conformation required for ATP hydrolysis to bring the lid helices into close proximity. Opening of the lid occurs in conjunction with releasing ADP from the active site. The complex can exist in an asymmetrical conformation with one ring closed and one open even during ATP cycling conditions, suggesting a inter-ring allosteric model mediated through a two-stroke mechanism. Molecular architecture of TRiC/CCT from the crystal structure, PDB ID 2XSM
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
individual subunits of TRiC have been shown to have protein-folding capacity
additional information
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
determination of kinetic intermediates in the sequential allosteric pathway of CCT/TRiC, kinetic mechanism and model, overview
additional information
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
the CCT2 subunit pair forms an unexpected Z shape. ATP binding induces a dramatic conformational change on the CCT2 side, thereby suggesting that CCT2 plays an essential role in TRiC allosteric cooperativity. The TRiC nucleotide cycle coordinates with its mechanical cycle in preparing folding intermediates for further productive folding, overview. The five ATP-binding subunits (CCT1-CCT4-CCT2-CCT5-CCT7) are located symmetrically around the on-axis CCT2 subunit in both rings and occupying one entire side of the complex. Accordingly, the ATP-driven conformational changes prixadmarily occur on that side. In contrast, the opposite CCT6 side of the complex (CCT8-CCT6-CCT3), most probably with ADP bound or partially occupying the nucleotide pocket, remains mostly poised in the ATP binding process. Thus, it appears that TRiC has evolved to be structurally divided into two sides. In addition, all of the sixteen subunits have their nucleotide pockets fully occupied in the further-refined yeast TRiC X-ray structure in the conformation with both rings tightly closed, thus suggesting that the subunits on the CCT6 side also have ATP-binding and ATP-hydrolysis abilities
additional information
-
the CCT2 subunit pair forms an unexpected Z shape. ATP binding induces a dramatic conformational change on the CCT2 side, thereby suggesting that CCT2 plays an essential role in TRiC allosteric cooperativity. The TRiC nucleotide cycle coordinates with its mechanical cycle in preparing folding intermediates for further productive folding, overview. The five ATP-binding subunits (CCT1-CCT4-CCT2-CCT5-CCT7) are located symmetrically around the on-axis CCT2 subunit in both rings and occupying one entire side of the complex. Accordingly, the ATP-driven conformational changes prixadmarily occur on that side. In contrast, the opposite CCT6 side of the complex (CCT8-CCT6-CCT3), most probably with ADP bound or partially occupying the nucleotide pocket, remains mostly poised in the ATP binding process. Thus, it appears that TRiC has evolved to be structurally divided into two sides. In addition, all of the sixteen subunits have their nucleotide pockets fully occupied in the further-refined yeast TRiC X-ray structure in the conformation with both rings tightly closed, thus suggesting that the subunits on the CCT6 side also have ATP-binding and ATP-hydrolysis abilities
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
TRiC redistributes to sites of viral replication. The TRiC chaperonin forms a complex with the reovirus sigma3 outer-capsid protein through an ATP-dependent mechanism
additional information
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
all CCT subunits are required for the CCT complex function
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
eight distinct subunits are uniquely organized, providing a favorable folding cavity for specific client proteins such as tubulin and actin. Because of its heterogeneous subunit composition, CCT complex has polarized inner faces, which may underlie an essential part of its chaperonin function. Molecular organization of the eukaryote chaperonin known as CCT/TRiC complex, overview. Dynamics-based structural profiling of asymmetrically oriented chaperonin function
additional information
-
eight distinct subunits are uniquely organized, providing a favorable folding cavity for specific client proteins such as tubulin and actin. Because of its heterogeneous subunit composition, CCT complex has polarized inner faces, which may underlie an essential part of its chaperonin function. Molecular organization of the eukaryote chaperonin known as CCT/TRiC complex, overview. Dynamics-based structural profiling of asymmetrically oriented chaperonin function
additional information
-
protein-folding mechanism mediated by group II chaperonins, overview. Asymmetry in the function and dynamics is shown by the cytosolic group II chaperonin CCT/TRiC. CtCCT subunits had similar characteristics in the ATP-binding pocket
additional information
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
enzyme structure homology modelling using the structure of TRiC/ADP (PDB ID 4A13, Bos taurus) and of GroES and GroEL/ES/ATP (PDB ID 1AON, Escherichia coli). Structure comparisons, overview
additional information
ATP hydrolysis is important to attain the closed conformation of the enzyme
additional information
analysis of molecular mechanisms of group II CPNs, ATP is involved in the protein folding inducing conformational changes of substrate and enzyme, overview
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview
additional information
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview. CCT protein recognition sequences and structure
additional information
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview
additional information
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview. The individual CCT subunits have different functions in cells. CCT-folding activity stalls at low ATP concentrations. Binding of the non-hydrolysable ATP analog adenosine 5'-(beta,gamma-imino)-triphosphate to the ternary complex leads to 3fold faster release of actin from CCT following the addition of ATP, suggesting a two-step folding process with a conformational change occurring upon closure of the cavity and a subsequent near-final folding step involving packing of the C-terminus to the native-like state. Proposed one-dimensional free-energy landscape for actin folding, overview. Actin folding and unfolding behaviour in vitro and thermodynamics
additional information
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
while AML1-175 is folded by TRiC to achieve its native function, ATP hydrolysis does not suffice to trigger its release from the chaperonin
additional information
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview
additional information
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview
additional information
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview
additional information
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview
additional information
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview. The Plasmodium falciparum actin proteins are more divergent compared with other eukaryotic actins, about 80% homologous, and so are their eight CCT complex and three phosducin-like cofactor proteins. CCT subunits and actin and tubulin are ART molecular target(s) in the asexual stages of the malaria parasite
additional information
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview
additional information
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
conformational dynamics of native and chaperonin-bound actin by equilibrium hydrogen/deuterium exchange-mass spectrometry, overview
additional information
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
structure-functional analysis, the three-dimensional structure of GaTRiC is modeled using the Saccharomyces cerevisiae TRiC structure (PDB ID 4V81) as template. Determination of ionic interactions of GaTRiC residues
additional information
-
structure-functional analysis, the three-dimensional structure of GaTRiC is modeled using the Saccharomyces cerevisiae TRiC structure (PDB ID 4V81) as template. Determination of ionic interactions of GaTRiC residues
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
human TRiC subunits interact with each other, but do not interact with export related parasite proteins from Plasmodium falciparum in extracts from trophozoite-stage infected red blood cells
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
substrate recognition by TRiC, binding and interaction structures, and reaction mechanism, overview. ATP hydrolysis drives the structural change of the TRiC complex. ATP-dependent conformational change originates in the high ATP affinity lobe of TRiC (CCT5/2/4/1). Chamber closure triggers substrate folding. TRiC releases its cargo upon ATP hydrolysis-induced conformational shifts. TRiC operates not only as a chaperone but also as a holdase, shielding substrates to prevent undesired activities until the appropriate conditions for their release are met. ATP-induced TRiC closure folds the substrate in collaboration with PhLP2A
additional information
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
substrate recognition by TRiC, binding and interaction structures, and reaction mechanism, overview. ATP hydrolysis drives the structural change of the TRiC complex. ATP-dependent conformational change originates in the high ATP affinity lobe of TRiC (CCT5/2/4/1). Chamber closure triggers substrate folding. TRiC releases its cargo upon ATP hydrolysis-induced conformational shifts. TRiC operates not only as a chaperone but also as a holdase, shielding substrates to prevent undesired activities until the appropriate conditions for their release are met. ATP-induced TRiC closure folds the substrate in collaboration with PhLP2A
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
ATP-driven cycle of TRiC-PFD-PhLP2A interaction: PhLP2A binds to open apo-TRiC through polyvalent domainspecific contacts with its chamber's equatorial and apical regions. PhLP2A N-terminal H3-domain binding to subunits CCT3/4 apical domains displace PFD from TRiC. ATP-induced TRiC closure rearranges the contacts of PhLP2A domains within the closed chamber. In the presence of substrate, actin and PhLP2A segregate into opposing chambers, each binding to positively charged inner surface residues from CCT1/3/6/8. Actin induces a conformational change in PhLP2A, causing its N-terminal helices to extend across the inter-ring interface to directly contact a hydrophobic groove in actin. Structure-function mechanism, detailed overview
additional information
-
analysis of ATP binding in the homo-oligomeric archaeal chaperonin from Methanococcus maripaludis (MmCpn), consisting of two stacked rings composed of eight identical subunits each, overview. Individual ATP binding events occur in a statistically random manner for MmCpn, both within and across the rings. ATP-induced heterogeneous conformational changes in the homo-oligomeric chaperonin MmCpn are determined by cryo-electronmicroscopy. Structure modelling, overview
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
nucleotide state of CCT in the mLST8-CCT complex, cryoEM structure analysis with resolution of 4.0 A, overview
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
chaperonins are large complexes about 1 MDa in size defined by a structure comprised of two stacked rings of 7-9 subunits with a protein folding chamber in the center of each ring. These subunits may be identical or homologous depending on the species. The cytosolic chaperonin containing TCP-1 (CCT or TRiC) is the Group II chaperonin in eukaryotic cells and the most complex of all the chaperonins. Its rings are composed of eight distinct subunits in a specific arrangement. The fact that most important substrates actin and tubulin bind to different sites is significant because it points to different CCT folding mechanisms for different proteins rather than a single universal folding mechanism
additional information
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
chaperonins are large complexes about 1 MDa in size defined by a structure comprised of two stacked rings of 7-9 subunits with a protein folding chamber in the center of each ring. These subunits may be identical or homologous depending on the species. The cytosolic chaperonin containing TCP-1 (CCT or TRiC) is the Group II chaperonin in eukaryotic cells and the most complex of all the chaperonins. Its rings are composed of eight distinct subunits in a specific arrangement. CCT is unique in that its subunits do not bind or hydrolyze ATP at equal rates. Instead, CCT is divided into two hemispheres; a high ATPase CCT2 hemisphere comprising CCT subunits 2, 4, 5, and 7, that drives ring closure, and a low ATPase CCT6 hemisphere, comprising CCT 1, 3, 6, 8. CCT 6 and 8 hardly bind ATP at physiological concentrations. The effect of this one-sided ATP hydrolysis is an asymmetric power stroke in which CCT closes its folding chamber sequentially in a defined order
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the hetero-oligomeric nature of TRiC is likely key to its unique ability to fold obligate substrates. Subunit divergence likely contributes to the folding process in various ways. The specific subunit arrangement segregates substrate and ATP binding properties within the ring and produces an asymmetric charge distribution within the closed chamber. Unfolded substrates such as actin, AML or VHL bind open TRiC through subunit specific contacts with CCT apical domains. ATP addition leads to lid closure and tubulin encapsulation and folding within the closed TRiC chamber
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
structure and conformation cycle mediated by TRiC/CCT, detailed overview. Molecular mechanisms underlying the functions of TRiC/CCT in Huntington's disease and myocardial infarction
additional information
-
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview
-
additional information
-
chaperonins are ubiquitous molecular chaperones with the subunit molecular mass of 60 kDa. They exist as double-ring oligomers with central cavities. An ATP-dependent conformational change of the cavity induces the folding of an unfolded protein that is captured in the cavity. Inter-ring communication is dispensable in the reaction cycle of group II chaperonins. Group II chaperonins do not require a co-chaperonin but have a built-in lid that is composed of a helical protrusion in the apical domain. The built-in lid seals off the central cavity and induces a conformational change to assist the folding of the trapped substrate, molecular mechanism analysis. Structure modeling of wild-type and mutant enzyme oligomers using structure of Thermococcus sp. JCM 11816, PDB ID 1Q2V, overview
-
additional information
-
determination of ATP-dependent dynamics of a group II chaperonin at the single-molecule level with highly accurate rotational axes views by UV light-triggered diffracted X-ray tracking, using caged-ATP and stopped-flow fluorometry. The closed ring twists counterclockwise and the twisted ring reverted to the original open-state with a clockwise motion, the biphasic lid-closure process occurs with unsynchronized closure and a synchronized counterclockwise twisting motion
-
additional information
-
reaction cycle model for group II chaperonins, ATP-binding, stopped-flow fluorometry and stopped-flow small-angle X-ray scattering, overview
-
additional information
-
group II chaperonins generally contain eight subunits per ring and have a tendency to heterooligomer formation. TRiC contains eight paralogous subunits per ring assembled in a defined order
-
additional information
-
determination of kinetic intermediates in the sequential allosteric pathway of CCT/TRiC, kinetic mechanism and model, overview
-
additional information
-
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview. The individual CCT subunits have different functions in cells. CCT-folding activity stalls at low ATP concentrations. Binding of the non-hydrolysable ATP analog adenosine 5'-(beta,gamma-imino)-triphosphate to the ternary complex leads to 3fold faster release of actin from CCT following the addition of ATP, suggesting a two-step folding process with a conformational change occurring upon closure of the cavity and a subsequent near-final folding step involving packing of the C-terminus to the native-like state. Proposed one-dimensional free-energy landscape for actin folding, overview. Actin folding and unfolding behaviour in vitro and thermodynamics
-
additional information
-
substrate recognition by TRiC, binding and interaction structures, and reaction mechanism, overview. ATP hydrolysis drives the structural change of the TRiC complex. ATP-dependent conformational change originates in the high ATP affinity lobe of TRiC (CCT5/2/4/1). Chamber closure triggers substrate folding. TRiC releases its cargo upon ATP hydrolysis-induced conformational shifts. TRiC operates not only as a chaperone but also as a holdase, shielding substrates to prevent undesired activities until the appropriate conditions for their release are met. ATP-induced TRiC closure folds the substrate in collaboration with PhLP2A
-
additional information
-
chaperonins are large complexes about 1 MDa in size defined by a structure comprised of two stacked rings of 7-9 subunits with a protein folding chamber in the center of each ring. These subunits may be identical or homologous depending on the species. The cytosolic chaperonin containing TCP-1 (CCT or TRiC) is the Group II chaperonin in eukaryotic cells and the most complex of all the chaperonins. Its rings are composed of eight distinct subunits in a specific arrangement. CCT is unique in that its subunits do not bind or hydrolyze ATP at equal rates. Instead, CCT is divided into two hemispheres; a high ATPase CCT2 hemisphere comprising CCT subunits 2, 4, 5, and 7, that drives ring closure, and a low ATPase CCT6 hemisphere, comprising CCT 1, 3, 6, 8. CCT 6 and 8 hardly bind ATP at physiological concentrations. The effect of this one-sided ATP hydrolysis is an asymmetric power stroke in which CCT closes its folding chamber sequentially in a defined order
-
additional information
-
structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview
-
additional information
-
three-dimensional structures of nucleotide states of thermosome and allosteric communications within the archaeal chaperonin thermosome, open and closed states and transitional conformation changes, computational analysis, overview
-
additional information
-
mechanisms and the structure-function relationships in the complex protein systems, structural dynamics, allostery, and associated conformational rearrangements, overview. Group II chaperonins cycle between an open, substrate-receptive conformation and a closed, substrate-trapping conformation, structure modeling, detailed overview
-
additional information
-
group II chaperonins cycle between an open, substrate-receptive conformation and a closed, substrate-trapping conformation, structure modeling, detailed overview
-
additional information
-
possesses two chaperonins, cold-inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high temperatures, respectively
-
additional information
-
chaperonins are ubiquitous molecular chaperones with the subunit molecular mass of 60 kDa. They exist as double-ring oligomers with central cavities. An ATP-dependent conformational change of the cavity induces the folding of an unfolded protein that is captured in the cavity. Inter-ring communication is dispensable in the reaction cycle of group II chaperonins. Group II chaperonins do not require a co-chaperonin but have a built-in lid that is composed of a helical protrusion in the apical domain. The built-in lid seals off the central cavity and induces a conformational change to assist the folding of the trapped substrate, molecular mechanism analysis. Structure modeling of wild-type and mutant enzyme oligomers using structure of Thermococcus sp. JCM 11816, PDB ID 1Q2V, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). THSB_THEK1
Thermococcus sp. (strain JCM 11816 / KS-1)
546
0
59174
Swiss-Prot
-
THS_PYRHO
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
549
0
59693
Swiss-Prot
-
TCPA_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
559
0
60481
Swiss-Prot
other Location (Reliability: 3)
THSA_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
545
0
58281
Swiss-Prot
Secretory Pathway (Reliability: 1)
THSB_THEAC
Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)
543
0
58480
Swiss-Prot
Secretory Pathway (Reliability: 1)
THSA_THEKO
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
548
0
59170
Swiss-Prot
-
THSA_THEK1
Thermococcus sp. (strain JCM 11816 / KS-1)
548
0
59170
Swiss-Prot
-
THSB_THEKO
Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
546
0
59158
Swiss-Prot
-
THSB_AERPE
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
548
0
60430
Swiss-Prot
-
THSA_AERPE
Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)
554
0
60374
Swiss-Prot
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
132000 - 240000
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
recombinant subunit LdTCP1epsilon as dimeric and tetrameric assembly, native PAGE
55000
-
10 * 55000, SDS-PAGE, assembles into a large ring-shaped oligomeric complex comprising about 10 subunits
550000
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
about, recombinant heterohexadecameric myc-tagged subunit theta complex, native PAGE
60000
60700
61200
900000
about, Mm-cpn protein complex, gel filtration and native PAGE
950000
-
purified recombinant CCT complex, about, sequence calculation
970000
-
purified recombinant CCT complex, about, gel filtration
60700
x * 60700 (subunit alpha) + x * 61200 (subunit beta), SDS-PAGE
60700
x * 60700 + x * 61200, alpha- and beta-subunits ApCpnA and ApCpnB, respectively, SDS-PAGE
61200
x * 60700 (subunit alpha) + x * 61200 (subunit beta), SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
-
10 * 55000, SDS-PAGE, assembles into a large ring-shaped oligomeric complex comprising about 10 subunits
heterohexadecamer
hexadecamer
octamer
oligomer
additional information
?
x * 60700 (subunit alpha) + x * 61200 (subunit beta), SDS-PAGE
heterohexadecamer
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
TRiC is a double-ringed structure composed of eight homologous but distinct subunits (CCT1-8)
heterohexadecamer
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
CCT is a large double-ring complex with a central cavity. Each ring is composed of eight paralogous subunits, CCT1-CCT8. All CCT subunits are required for the CCT complex function
heterohexadecamer
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
eukaryotic cytoplasmic chaperonin TCP/TRiC/CCT forms a barrel-like structure, which is composed of 8 related subunits that are each present twice
heterohexadecamer
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
TRiC forms a high molecular weight heterohexadecamer, comprised of two eight-membered rings
heterohexadecamer
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
TRiC is a double-ringed structure composed of eight homologous but distinct subunits (CCT1-8)
heterohexadecamer
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol. TRiC is a class II chaperonin, which typically forms a high molecular weight heterohexadecamer, comprised of two eight-membered rings
heterohexadecamer
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the hetero-oligomeric complex has a double-chamber architecture, with each octameric ring formed by subunits CCT1-8
heterohexadecamer
-
a dimer of octamers, the homo-oligomeric archaeal group II chaperonin from Methanococcus maripaludis (MmCpn) consists of two stacked rings stacked back-to-back composed of eight identical subunits each. While the fully closed state induced by ATP hydrolysis is eight-fold symmetrical, the ATP-bound states can have different and heterogeneous conformations, depending on whether ATP occupies that particular subunit. Focused classification of conformational heterogeneity, overview
heterohexadecamer
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol. TRiC is a class II chaperonin, which typically forms a high molecular weight heterohexadecamer, comprised of two eight-membered rings. PfTRiC forms a large complex in the parasite cytosol
heterohexadecamer
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
the PfCCT complex forms a heterohexadecamer, a dimer of octamers. CCT is constructed from two identical, but opposed, rings made by eight independent subunits, encoded by eight homologous genes, and positioned in each ring in a precise arrangement. Each CCT subunit consists of three domains: the equatorial domain harboring the ATP binding site, an intermediate domain, and the apical domain involved in substrate binding. The specific sequence differences between the eight CCT subunits are located mainly in their apical domains which provide the substrate binding specificity of each subunit
heterohexadecamer
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
-
heterohexadecamer
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
dimer of octamers, analysis of subunit locations in open-state TRiC by inner-subunit eGFP tagging, overview. TRiC has a double-ring structure, and each ring consists of eight homologous but distinct subunits arranged in a specific order
heterohexadecamer
-
CCT is composed of 8 different paralogous subunits, two octamers form a ring structure, a complicated structure
octamer
-
unique asymmetric pattern among the eight subunits of TRiC in the nucleotide-free state, mechanism of TRiC negative inter-ring cooperativity. The TRiC lid remains open in three states of the cycle: ATP bound, ADP bound, and nucleotide free, structure-function relationship, structure modeling and electron cryo-microscopy, overview
octamer
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
molecular organization of the eukaryote chaperonin known as CCT/TRiC complex, overview. Analysis of closed and open states of CCT complex, using molecular dynamics. The inter-subunit interaction energies are asymmetrically distributed and are remodeled during conformational changes of CCT complex. Exploration of redox related characteristics indicate changes in inner surface properties, including electrostatic potential, pKa and exposure of inner cysteine thiol groups, between the closed and open states
octamer
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta encoded by genes CCT1-8
octamer
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
TRiC/CCT is a 1-MDa hetero-oligomer consisting of two stacked octameric rings that fold proteins in a manner dependent on ATP hydrolysis, architecture and overall structure of TRIC/CCT, structure and conformational cycle of the TRiC/CCT complex, detailed overview
octamer
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
60000 Da subunit LdTCP1epsilon exhibits significant differences in the primary structure as compared to LdTCP1gamma and is evolutionary close to LdTCP1 zeta subunit
octamer
-
60000 Da subunit LdTCP1epsilon exhibits significant differences in the primary structure as compared to LdTCP1gamma and is evolutionary close to LdTCP1 zeta subunit
-
octamer
Leishmania donovani MHOM/IN/80
-
60000 Da subunit LdTCP1epsilon exhibits significant differences in the primary structure as compared to LdTCP1gamma and is evolutionary close to LdTCP1 zeta subunit
-
octamer
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
CCT1-8 subunits form the CCT
oligomer
-
subunit arrangement of the hetero-oligomeric eukaryotic chaperonin TRiC
additional information
the cooperativity of alpha- and beta-subunits is investigated
additional information
-
the cooperativity of alpha- and beta-subunits is investigated
additional information
x * 60700 + x * 61200, alpha- and beta-subunits ApCpnA and ApCpnB, respectively, SDS-PAGE
additional information
x * 60700 + x * 61200, alpha- and beta-subunits ApCpnA and ApCpnB, respectively, SDS-PAGE
additional information
x * 60700 + x * 61200, alpha- and beta-subunits ApCpnA and ApCpnB, respectively, SDS-PAGE
additional information
-
the cooperativity of alpha- and beta-subunits is investigated
-
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
monomeric subunit CCT1 has a molecular weight of about 60 kDa
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
both subunits CCT4 and CCT5 can be assembled into homomeric hexadecamers which allow them to be studied individually in the context of an assembled ring system
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
although the CCT subunits carry only 27%-39% identical sequences, their secondary structures are very similar. The ATP-binding domain is the most conserved domain across CCT subunits, while the substrate-binding domain varies across subunits. Each subunit consists of three domains: the apical domain comprising the top of the ring, which recognises a substrate and forms a lid; the equatorial domain, which contains an ATP-binding site, and the intermediate domain, which is indispensable for ATP hydrolysis and ATP cycling
additional information
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
the theta subunit has a molecular weight of 60.9 kDa. The plasmodial subunit theta can form high molecular weight complexes in the parasite soluble fraction. Loss of one subunit (PfTRiC-theta) in the heterohexadecamer is disrupts formation of the entire complex
additional information
-
the theta subunit has a molecular weight of 60.9 kDa. The plasmodial subunit theta can form high molecular weight complexes in the parasite soluble fraction. Loss of one subunit (PfTRiC-theta) in the heterohexadecamer is disrupts formation of the entire complex
additional information
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
both subunits CCT4 and CCT5 can be assembled into homomeric hexadecamers which allow them to be studied individually in the context of an assembled ring system
additional information
-
both subunits CCT4 and CCT5 can be assembled into homomeric hexadecamers which allow them to be studied individually in the context of an assembled ring system
-
additional information
-
CCT is composed of 8 different paralogue subunits. They are designated CCT1, CCT2, CCT3, CCT4 CCT5, CCT6, CCT7 and CCT8. They are also named CCTalpha, CCTbeta, CCTgamma, CCTdelta, CCTepsilon, CCTzeta, CCTeta, and CCTtheta. CCT subunits share a high amino acid similarity in the phosphate binding loop and the catalytic site but have a low amino acid sequence similarity in the nucleotide binding site, and they may generate variation in ATP binding and hydrolysis capability
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
phosphoprotein
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
InR/PI3K/Akt network in Drosophila dynamically phosphorylates sbunit CCT8 in response to insulin stimulation
ubiquitination
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
VRK2 is important for the eukaryotic chaperonin TRiC protein degradation pathway and is involved in polyQ protein aggregation. Ubiquitin-specific protease 25 (USP25) is a VRK2 substrate that acts on TRiC deubiquitination. USP25 deubiquitinates TRiC subunit CCT4. TRiC ubiquitination is induced by inhibition of USP25 and E3 ligase COP1 is recruited. Subsequently, TRiC protein levels are decreased. USP25 knockdown enhances CCT4 polyubiquitination and reduces CCT4 protein levels
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure analysis of the open conformation of the mammalian chaperonin CCT in complex with tubulin, overview
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
cryo-specimen preparation of AML-1-ETO DNA-binding domain (AML1-175), with TRiC and Hsp70, and cryo-EM imaging, three-dimensional cryo-EM map reconstruction, modelling, method, overview. TRiC can refold denatured AML1-175 (DBD) and restore its DNA binding activity in vitro. Reconstructed the TRiC-AML1-175 complex forms in the presence of Ni2+-gold nanoparticles capable of binding to the His-tag on AML1-175. Ni-affinity nanogold particles reveal the location of AML1-175 on TRiC
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
structure analysis of the open conformation of the mammalian chaperonin CCT in complex with tubulin, overview
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
crystal structure analysis, PDB IDs 3IYF and 3LOS, enzyme in open and closed state conformation
-
homology model of the FAB1 apical domain and the top scoring model was with the 2.2 A resolution mouse CCTgamma apical domain template, PDB ID 1GML
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
cryo-EM structures of Saccharomyces cerevisiae TRiC in a nucleotide partially preloaded (NPP) state and in the ATP-bound state at 4.7 A and 4.6 A resolution, respectively
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
recombinant enzyme, removal of all surface exposed cysteine residues for diffracted X-ray tracking experiment, and addition of cysteine residues at the tip of helical protrusions of selected two subunits. Gold nanocrystals are attached onto CtCCTs via gold-thiol bonds and applied for the analysis by diffracted X-ray tracking
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
H147R
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
naturally occuring mutation of subunit CCT5
D386A
site-directed mutagenesis, introduction of D386A into Mm-cpn significantly reduces its ability to complement for loss of GroES and GroEL, loss of ATPase activity severely affects the complementing ability of the wild-type and mutant Mm-cpn proteins
G160S
-
the TRiC-like mutant G160S of MmCpn has a drastically slower rate of ATP hydrolysis, roughly equivalent to the steady-state hydrolysis of eukaryotic TRiC
K216A
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216C
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216D
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216E
random mutagenesis, growth for the mutants is clearly faster than for wild-type Mm-cpn organisms under GroES/GroEL-limiting conditions, improved phenotype in Escherichia coli under GroEL- and GroES-depleting conditions. The mutant can effectively hydrolyze ATP
K216E/D386A
site-directed mutagenesis, introduction of D386A into Mm-cpn significantly reduces its ability to complement for loss of GroES and GroEL, loss of ATPase activity severely affects the complementing ability of the wild-type and mutant Mm-cpn proteins
K216F
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216G
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216L
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216P
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216Q
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216R
site-directed mutagenesis, the mutant enzyme slightly complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216S
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216T
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
K216V
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
K216Y
site-directed mutagenesis, the mutant enzyme moderately complements the GroEL-deletion mutant Escherichia coli strain TAB21
M223E
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223F
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223G
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223I
M223I/D386A
site-directed mutagenesis, introduction of D386A into Mm-cpn significantly reduces its ability to complement for loss of GroES and GroEL, loss of ATPase activity severely affects the complementing ability of the wild-type and mutant Mm-cpn proteins
M223L
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223R
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223S
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223V
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223W
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
M223Y
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
C450Y
G345D
D545G
site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA
D545M
site-directed mutagenesis, the mutant shows slightly higher stabilities than that of wild-type CpkA
E530G
site-directed mutagenesis, the mutant strain DA4 shows increased ATPase activity. The CpkA-E530G mutation prevents cold denaturation of proteins under cold-stress conditions, thereby enabling cells to grow in cooler environments
E530M
site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA
P538G
site-directed mutagenesis, the mutant shows slightly higher stabilities than that of wild-type CpkA
P538M
site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA
Q533M
site-directed mutagenesis, the mutant shows a stabilities similar to the wild-type CpkA
D64A/D393A
site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change
D64A/D393A/K485W
site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change, the mutant lacks ATP-dependent refolding activity, nucleotide binding and ATP-dependent conformational change kinetics, overview
K165A/K485W
site-directed mutagenesis, ATPase inactive mutant that can partially prevent the spontaneous refolding ofGFP and refold it in an ATP-dependent manner
K485W
L265W
site-directed mutagenesis, replacement of amino acid L265 with Trp partially impairs the protein folding activity, eight Trp residues are thought to come close in the closed conformation. The resulting steric hindrance might interrupt the conformational changes required for protein folding. Although ATP hydrolysis activity is almost completely lost in the absence of K+, slight ATP-dependent folding activity is observed
L56W
site-directed mutagenesis, the mutant exhibits nearly the same level of protein folding activity as the wild-type protein
D64A/D393A
-
site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change
-
D64A/D393A/K485W
-
site-directed mutagenesis, an ATPase-deficient mutant, the mutant also does not exhibit ATPase-dependent conformational change, the mutant lacks ATP-dependent refolding activity, nucleotide binding and ATP-dependent conformational change kinetics, overview
-
K165A/K485W
-
site-directed mutagenesis, ATPase inactive mutant that can partially prevent the spontaneous refolding ofGFP and refold it in an ATP-dependent manner
-
K485W
L265W
-
site-directed mutagenesis, replacement of amino acid L265 with Trp partially impairs the protein folding activity, eight Trp residues are thought to come close in the closed conformation. The resulting steric hindrance might interrupt the conformational changes required for protein folding. Although ATP hydrolysis activity is almost completely lost in the absence of K+, slight ATP-dependent folding activity is observed
-
L56W
-
site-directed mutagenesis, the mutant exhibits nearly the same level of protein folding activity as the wild-type protein
-
K165A/K485W
-
site-directed mutagenesis, ATPase inactive mutant that can partially prevent the spontaneous refolding ofGFP and refold it in an ATP-dependent manner
-
K485W
-
site-directed mutagenesis, the mutant shows ATP binding and conformational change upon ATP binding
-
additional information
M223I
random mutagenesis, growth for the mutants is clearly faster than for wild-type Mm-cpn organisms under GroES/GroEL-limiting conditions, improved phenotype in Escherichia coli under GroEL- and GroES-depleting conditions. The mutant can effectively hydrolyze ATP
M223I
site-directed mutagenesis, the mutant enzyme complements the GroEL-deletion mutant Escherichia coli strain TAB21 well
C450Y
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
naturally occuring mutation in subunit CCT4
G345D
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
site-directed mutagenesis in subunit CCT4 decreases cooperativity in ATP binding compared to wild-type
G345D
-
site-directed mutagenesis in subunit CCT4 decreases cooperativity in ATP binding compared to wild-type
-
K485W
site-directed mutagenesis, the mutant shows ATP binding and conformational change upon ATP binding
K485W
site-directed mutagenesis, the mutant lacks ATP-dependent refolding activity, nucleotide binding and ATP-dependent conformational change kinetics, overview
K485W
-
site-directed mutagenesis, the mutant shows ATP binding and conformational change upon ATP binding
-
K485W
-
site-directed mutagenesis, the mutant lacks ATP-dependent refolding activity, nucleotide binding and ATP-dependent conformational change kinetics, overview
-
additional information
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
a missense mutation in cct5 causes muscle impairment within cct5tf212b, mapping of tf212b links the phenotype-causing mutation to the gene encoding the TRiC subunit Cct5 on chromosome 24, severe reduction in the amount of myofibrils. Knockdown of cct5 by two independent morpholinos, both validated for their functionality, results in a reduction of birefringence comparable with cct5tf212b homozygotes. A second mutant allele of cct5, cct5hi2972Tg, carries a single retroviral insertion in cct5 and fails to complement the bire-fringence reduction of cct5tf212b. In addition, both cct5 mutants are significantly ameliorated by injection of full-length cct5 mRNA, confirming that the phenotype-causing mutation of cct5tf212b resides within cct5. In addition to the trunk muscle, the head musculature of cct5tf212b mutants is also affected. Mutations in other TRiC subunits, e.g. CCT3 or CCT4, also cause impaired myofibril assembly. Mutants cct3sa1761 and cct4x0114 null develop into relatively normal larvae that exhibit skeletal muscle defects grossly similar to the other cct mutants
additional information
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
gene CCT4 is knocked down by RNAi (v106099) in eye discs by using ey-Gal4 that drives GAL4 expression in eye and head primordia, all progeny die during the late pupal stage. Similar results are obtained by an additional CCT4 RNAi line (5525R-3). Dead flies in pupal cases have relatively intact thorax and abdomen but completely lack the eye-head structures. The eye-head field in larval eye discs targeted by ey-Gal4 is lost, resulting in the headless phenotype and late pupal lethality. Loss of any CCT subunit leads to similar loss-of-function phenotypes by disrupting the function of the CCT complex in vivo. Mutant phenotype, overview
additional information
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
knockdown of each cct subunit gene in the prothoracic gland (PG). Cell number and C value in the mutant PG are increased compared to wild-type. Usage of an PG-selective RNAi screen to identify MES regulator(s). A statistically significant difference occurs in pH3 expression between control and cct RNAi. cct genes are also required for proper progression of mitotic cell cycle, development is mainly arrested at the L3 stage in cct RNAi animals (phm>cct-RNAi). Ecdysteroidogenic gene expression is significantly reduced in cct RNAi, and 20E administration restores larval-to-pupal transition in 20-30% of animals
additional information
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
cardiac-specific knockdown of chaperonin CCT in Drosophila melanogaster resulting in disorganization of cardiac actin- and myosin-containing myofibrils and severe physiological dysfunction, including restricted heart diameters, elevated cardiac dysrhythmia and compromised cardiac performance. Knockdown of Cct3, Cct4, Cct5, Cct6 or Cct7 with the TinCDELTA4 driver resulted in cardiac morphological defects in one or more non-beating regions of the heart and completely non-beating hearts. These defects are not observed with TinC/+. Moreover, defects are even more severe with knockdown of Cct3, Cct4, Cct5, Cct6 or Cct7 with the Hand-Gal4 driver, whereas Hand/+ hearts do not show these defects.In addition to cardiac defects, cardiac-specific knockdown of Cct3, Cct4, Cct5, Cct6 or Cct7 has a drastic impact on the lifespan of the flies (female and male combined) compared to TinCDELTA4/+ and Hand/+ flies. Extremely severe cardiac dysfunction observed with Hand/+ upon cardiac-specific knockdown of Cct3, Cct4, Cct5, Cct6 or Cct7, correlate with further shortening of lifespan compared to TinCDELTA4/+. Quantitative analysis of additional cardiac physiological parameters, mutant phenotypes, overview
additional information
-
knockdown of each cct subunit gene in the prothoracic gland (PG). Cell number and C value in the mutant PG are increased compared to wild-type. Usage of an PG-selective RNAi screen to identify MES regulator(s). A statistically significant difference occurs in pH3 expression between control and cct RNAi. cct genes are also required for proper progression of mitotic cell cycle, development is mainly arrested at the L3 stage in cct RNAi animals (phm>cct-RNAi). Ecdysteroidogenic gene expression is significantly reduced in cct RNAi, and 20E administration restores larval-to-pupal transition in 20-30% of animals
-
additional information
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
three categories of residue substitutions are found in alpha, beta, and gamma subunits: (i) bulky/polar side chains to alanine or valine, (ii) charged residues to alanine, and (iii) isoleucine to valine that is expected to increase intramolecular flexibility within the GaTRiC
additional information
-
three categories of residue substitutions are found in alpha, beta, and gamma subunits: (i) bulky/polar side chains to alanine or valine, (ii) charged residues to alanine, and (iii) isoleucine to valine that is expected to increase intramolecular flexibility within the GaTRiC
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
RNAi based gene knockout via shRNA expressing lentivirus constructs. Analysis of overexpressed genes playing a role in mediating the growth and survival of SUM-52 breast cancer cells via large-scale RNAi-based growth and viability screen, overview. RNAi-mediated knockdown targeting CCT2 inhibits growth and colony formation of SUM-52 breast cancer cells. Knocking downTCP1 has a cell-type-specific effect on cell growth and colony forming capacity in SUM-52 cells
additional information
-
RNAi based gene knockout via shRNA expressing lentivirus constructs. Analysis of overexpressed genes playing a role in mediating the growth and survival of SUM-52 breast cancer cells via large-scale RNAi-based growth and viability screen, overview. RNAi-mediated knockdown targeting CCT2 inhibits growth and colony formation of SUM-52 breast cancer cells. Knocking downTCP1 has a cell-type-specific effect on cell growth and colony forming capacity in SUM-52 cells
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
LCMV growth is significantly inhibited in cells transduced with shRNA specific for TCP1, CCT4, CCT5, CCT6, or CCT7, with highest degree of LCMV inhibition observed in cells transduced with shRNAs to TCP1, CCT5, and CCT7. Gene knockdown by shRNA. For knockdown in HEK-293T cells, cells are transfected with pGFP-CshLenti-targeting TCP1, CCT2-8
additional information
generation of SCC-15 and HSC-3 cells overexpressing CCT6A, or of SCC-15 and HSC-3 cells with CCT6A knockout. Wnt4 overexpression or Notch1 overexpression plasmids are transfected into CCT6A-knockout SCC-15 cells. Cell proliferation, apoptosis, invasion, stemness, Notch, and Wnt pathways are detected in both cell lines, whereas RNA sequencing is only performed in SCC-15 cells. CCT6A is upregulated in five OSCC cell lines, including SCC-15, HSC-3, SAT, SCC-9, and KON, compared to that in the control cell line. In SCC-15 and HSC-3 cells, CCT6A overexpression increases cell proliferation, invasion, sphere formation, CD133, and Sox2 expression, but decreases cell apoptosis, while CCT6A knockout exhibits an opposite effect on the above indexes. Activation of the Wnt or Notch pathways attenuates the effect of CCT6A knockout on SCC-15 cell survival, invasion, and stemness
additional information
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
CCT complex depletion by siRNA transfection in U2OS cells with dox-inducible A3A transgenes leads to decreased cell viability when A3A is expressed. Cytotoxicity from A3A is increased upon CCT depletion. A3A mutational signatures are enriched in cancers with deleterious CCT mutations
additional information
summary of the functional growth analysis of Escherichia coli TAB21 cells expressing diverse Mm-cpn-M223 and Mm-cpn-K216 mutants at 30°C, overview. The Mm-cpn-K216E and Mm-cpn-M223I mutants act as genuine chaperonins and must complete an ATP-dependent chaperonin cycle to function in Escherichia coli
additional information
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
generation of CCT1 and/or CCT5 KO 3T3-L1 cells by siRNA expression
additional information
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
generation of a regulatable PfTRiC-theta line expressing Myc-tagged subunit theta that forms a large complex in the parasite cytosol, and a theta subunit knockout line. The PfTRiC-theta-MYC clones retain between 4 and 10 aptamer elements. Knockout of PfTRiC-alpha and -zeta subunits using double homologous recombination
additional information
-
generation of a regulatable PfTRiC-theta line expressing Myc-tagged subunit theta that forms a large complex in the parasite cytosol, and a theta subunit knockout line. The PfTRiC-theta-MYC clones retain between 4 and 10 aptamer elements. Knockout of PfTRiC-alpha and -zeta subunits using double homologous recombination
additional information
-
generation of CtCCT variants containing ATPase-deficient subunits. Removal of all surface exposed cysteine residues for diffracted X-ray tracking experiment, and addition of cysteine residues at the tip of helical protrusions of selected two subunits. Gold nanocrystals are attached onto CtCCTs via gold-thiol bonds and applied for the analysis by diffracted X-ray tracking. Irrespective of the locations of cysteines, ATP binding induces tilting motion followed by rotational motion in the CtCCT molecule, like the archaeal group II chaperonins. When gold nanocrystals are attached onto two subunits in the high ATPase activity hemisphere, the CtCCT complex exhibits a fairly rapid response to the motion. In contrast, the response of CtCCT, which has gold nanocrystals attached to the low-activity hemisphere, is slow. Change from an open to a closed state using caged-ATP, which is a derivative of ATP that is inactive and does not bind to the ATP binding site of the chaperonin
additional information
construction of gene cpkA disruption mutant strains. Gene disruptant strain DA1 (DELTAcpkA) shows decreased cell growth at 60°C as compared to 85°C for the wild-type strain KOD1. The DB2 mutant (DELTAcpkA::cpkB DELTAcpkB), whose cpkB gene is expressed under the control of the cpkA promoter, does not grow at 60°C, and the DB3 mutant (DELTAcpkA(1-524)::cpkB(1-524) DELTAcpkB), whose CpkA amino acid residues 1 to 524 are replaced with corresponding CpkB residues that maintains the C-terminal region intact, grows at 60°C, implying that the CpkA C-terminal region plays a key role in cell growth at 60°C. Proteins coimmunoprecipitated with anti-Cpk from DB1 cells cultivated at 60°C, overview
additional information
construction of gene cpkA disruption mutant strains. Gene disruptant strain DA1 (DELTAcpkA) shows decreased cell growth at 60°C as compared to 85°C for the wild-type strain KOD1. The DB2 mutant (DELTAcpkA::cpkB DELTAcpkB), whose cpkB gene is expressed under the control of the cpkA promoter, does not grow at 60°C, and the DB3 mutant (DELTAcpkA(1-524)::cpkB(1-524) DELTAcpkB), whose CpkA amino acid residues 1 to 524 are replaced with corresponding CpkB residues that maintains the C-terminal region intact, grows at 60°C, implying that the CpkA C-terminal region plays a key role in cell growth at 60°C. Proteins coimmunoprecipitated with anti-Cpk from DB1 cells cultivated at 60°C, overview
additional information
construction of gene cpkB disruption mutant strains. Gene disruptant strain DB1 (DELTAcpkB) shows decreased cell growth at 93°C as compared to 85°C for the wild-type strain KOD1. The DB2 mutant (DELTAcpkA::cpkB DELTAcpkB), whose cpkB gene is expressed under the control of the cpkA promoter, does not grow at 60°C, and the DB3 mutant (DELTAcpkA(1-524)::cpkB(1-524) DELTAcpkB), whose CpkA amino acid residues 1 to 524 are replaced with corresponding CpkB residues that maintains the C-terminal region intact, grows at 60°C, implying that the CpkA C-terminal region plays a key role in cell growth at 60°C. Proteins coimmunoprecipitated with anti-Cpk from DB1 cells cultivated at 60°C, overview
additional information
construction of gene cpkB disruption mutant strains. Gene disruptant strain DB1 (DELTAcpkB) shows decreased cell growth at 93°C as compared to 85°C for the wild-type strain KOD1. The DB2 mutant (DELTAcpkA::cpkB DELTAcpkB), whose cpkB gene is expressed under the control of the cpkA promoter, does not grow at 60°C, and the DB3 mutant (DELTAcpkA(1-524)::cpkB(1-524) DELTAcpkB), whose CpkA amino acid residues 1 to 524 are replaced with corresponding CpkB residues that maintains the C-terminal region intact, grows at 60°C, implying that the CpkA C-terminal region plays a key role in cell growth at 60°C. Proteins coimmunoprecipitated with anti-Cpk from DB1 cells cultivated at 60°C, overview
additional information
construction of the asymmetric ring complex of a group II chaperonin using circular permutated covalent mutants, TKS1-CPNASR. Although one ring of the asymmetric ring complex lacks ATPase or ATP binding activity, the other wild-type ring undergoes an ATP-dependent conformational change and maintains protein-folding activity. It is possible to construct covalent chaperonin complexes by connecting N and C-termini. Circular permutated covalent enzyme TKS1-CPN (CPNCPC) is constructed by applying circular permutation to the covalent TKS1-CPN dimer, the circular permutated covalent TKS1-CPN dimer that has the deletion of 95 amino acids from its N-terminus and the addition of the same 95 amino acids to its C-terminus can assemble into a doublering structure similar to the wild-type. The 95th amino acid residue is located at the loop region between Helix 4 and Helix 5. The complex of the TKS1-CPN variant has ann molecular weight of approximately 120 kDa determined by SDS-PAGE. The ATPase activity of mutant CPNASR is half that of the recombinant His-tagged CPNwild-type homooligomer. Phenotypes, overview
additional information
construction of the asymmetric ring complex of a group II chaperonin using circular permutated covalent mutants, TKS1-CPNASR. Although one ring of the asymmetric ring complex lacks ATPase or ATP binding activity, the other wild-type ring undergoes an ATP-dependent conformational change and maintains protein-folding activity. It is possible to construct covalent chaperonin complexes by connecting N and C-termini. Circular permutated covalent enzyme TKS1-CPN (CPNCPC) is constructed by applying circular permutation to the covalent TKS1-CPN dimer, the circular permutated covalent TKS1-CPN dimer that has the deletion of 95 amino acids from its N-terminus and the addition of the same 95 amino acids to its C-terminus can assemble into a doublering structure similar to the wild-type. The 95th amino acid residue is located at the loop region between Helix 4 and Helix 5. The complex of the TKS1-CPN variant has ann molecular weight of approximately 120 kDa determined by SDS-PAGE. The ATPase activity of mutant CPNASR is half that of the recombinant His-tagged CPNwild-type homooligomer. Phenotypes, overview
additional information
construction of three CPNbeta mutants, with the truncation of 1, 2 and 6 amino acids from the C-terminus, named CPNbetaTc1, CPNbetaTc2 and CPNbetaTc6, respectively. CPNbetaTc2 and CPNbetaTc6 are designed to delete two hydrophobic amino acid residues from the CPNbeta C-terminus (Gly-Ser-Glu-Asp-/Phe-Gly-Ser-Asp-/Leu-Asp, with / indicating Tc6 and Tc2 truncation positions). The mutants form hexadecameric homooligomers, similar to the wild-type CPNbeta (CPNbetaWT). The thermal aggregation of CS is completely suppressed by the presence of an equimolar amount of the CPNbeta mutant variants. The truncation mutants exhibit the same protection abilities as CPNbetaWT. The mutant isoforms CPNbeta and PFDalpha1beta1 from strain KS1 interact with each other at high affinity, interaction analysis using immobilized PFDalpha1beta1, overview
additional information
-
construction of the asymmetric ring complex of a group II chaperonin using circular permutated covalent mutants, TKS1-CPNASR. Although one ring of the asymmetric ring complex lacks ATPase or ATP binding activity, the other wild-type ring undergoes an ATP-dependent conformational change and maintains protein-folding activity. It is possible to construct covalent chaperonin complexes by connecting N and C-termini. Circular permutated covalent enzyme TKS1-CPN (CPNCPC) is constructed by applying circular permutation to the covalent TKS1-CPN dimer, the circular permutated covalent TKS1-CPN dimer that has the deletion of 95 amino acids from its N-terminus and the addition of the same 95 amino acids to its C-terminus can assemble into a doublering structure similar to the wild-type. The 95th amino acid residue is located at the loop region between Helix 4 and Helix 5. The complex of the TKS1-CPN variant has ann molecular weight of approximately 120 kDa determined by SDS-PAGE. The ATPase activity of mutant CPNASR is half that of the recombinant His-tagged CPNwild-type homooligomer. Phenotypes, overview
-
additional information
-
construction of the asymmetric ring complex of a group II chaperonin using circular permutated covalent mutants, TKS1-CPNASR. Although one ring of the asymmetric ring complex lacks ATPase or ATP binding activity, the other wild-type ring undergoes an ATP-dependent conformational change and maintains protein-folding activity. It is possible to construct covalent chaperonin complexes by connecting N and C-termini. Circular permutated covalent enzyme TKS1-CPN (CPNCPC) is constructed by applying circular permutation to the covalent TKS1-CPN dimer, the circular permutated covalent TKS1-CPN dimer that has the deletion of 95 amino acids from its N-terminus and the addition of the same 95 amino acids to its C-terminus can assemble into a doublering structure similar to the wild-type. The 95th amino acid residue is located at the loop region between Helix 4 and Helix 5. The complex of the TKS1-CPN variant has ann molecular weight of approximately 120 kDa determined by SDS-PAGE. The ATPase activity of mutant CPNASR is half that of the recombinant His-tagged CPNwild-type homooligomer. Phenotypes, overview
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
thermal unfolding plots for recombinant wild-type and mutant enzymes. The thermal unfolding plots for mutants E530M, Q533M, P538M, and D545G are very similar to that for wild-type CpkA. CpkA mutants E530G and Q533M show slightly lower thermal stabilities, while CpkA mutants P538G and D545M show slightly higher stabilities than that of wild-type CpkA
additional information
thermal unfolding plots for recombinant wild-type and mutant enzymes. The thermal unfolding plots for mutants E530M, Q533M, P538M, and D545G are very similar to that for wild-type CpkA. CpkA mutants E530G and Q533M show slightly lower thermal stabilities, while CpkA mutants P538G and D545M show slightly higher stabilities than that of wild-type CpkA
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
Vaccinia-related kinase 2 controls the stability of the eukaryotic chaperonin TRiC/CCT by inhibiting the deubiquitinating enzyme USP25
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CCT complexes are extracted from infected human erythrocyte cultures synchronized for maximum expression levels of CCT at the trophozoite stage of the parasite's asexual life cycle, purification of recombinant C-terminally FLAG-tagged CCT8 subunits from transfected parasites by affinity chromatography and sucrose gradient fractionation
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
each of the recombinant alpha- and beta- subunits is purified to 92% and 94% by using anion exchange chromatography
native enzyme by anion exchange chromatography and gel filtration
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
native enzyme by calmodulin affinity chromatography and gel filtration
P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
native enzyme from bovine testes by anion exchange chromatography and gel filtration
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
native enzyme from HeLa cells by anion exchange chromatography and gel filtration
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
native enzyme is purified from HeLa cells by a process including anion exchange chromatography and gel filtration
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
recombinant alpha-subunit from Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) by heat shock treatment and anion exchange chromatography
recombinant beta-subunit from Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) by heat shock treatment and anion exchange chromatography
recombinant chaperonin Mm-cpn from Escherichia coli strain BL21(DE3) by anion exchange chromatography, ammonium sulfate fractionation, and gel filtation, followed by ultrafiltration
recombinant enzyme CPN from Escherichia coli strain BLR(DE3)/pET23a by heat treatment for 15 min at 90°C, anion exchange chromatography, ultrafiltration, and gel filtration
-
recombinant enzyme MmCpn from Escherichia coli strain Rosetta (DE3) pLys by ammonium sulfate fractionation, dialysis, and anion exchange chromatography, followed by heparin affinity chromatography, ultrafiltration, gel filtration, and again ultrafiltration
-
recombinant His-tagged TRiC with GFP-tagged CCT1 from High Five insect cells by benzonase treatment, nickel affinity and heparin affinity chromatography, followed by anion exchange chromatography, gel filtration, and ultrafiltration
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
recombinant His-tagged wild-type and mutant enzyme oligomer rings from Escherichia coli
recombinant Strep-tagged wild-type and mutant CCT complexes from Escherichia coli strain BL21 Star(DE3)pRARE by affinity and anion exchange chromatography, and gel filtration
-
recombinant wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) RIL by heat treatment at 85°C for 30 min, anion exchange chromatography, and gel filtration
the recombinant enzyme is purified to 91% by heat-shock treatment and anion-exchange chromatography
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ApCpnA and ApCpnB chaperonin genes are overexpressed in Escherichia coli Rosetta and Codonplus (DE3), respectively
expression of ApCpnA (subunit alpha) and ApCpnB (subunit beta) in Escherichia coli Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3) cells
gene CCT1-8, cloning of mouse testis CCT genes
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
gene CCT8, recombinant overexpression of the C-terminally FLAG-tagged CCT8 subunit in Plasmodium falciparum parasites propagated in human erythrocytes, wild-type parasites are unable to grow whereas parasites containing the plasmid (containing a hDHFR positive selection cassette) are able to grow. Isolated expression of FLAG-tagged CCT1 and CCT8 in parasites at endogenous levels
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
gene cpkA, recombinant expression of the chimeric chaperonin CpkBA in Escherichia coli
gene cpkB, recombinant expression of the chimeric chaperonin CpkBA in Escherichia coli
gene thsA, recombinant expression of alpha-subunit in Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3)
gene thsB, recombinant expression of beta-subunit in Escherichia coli strains Rosetta (DE3), BL21 (DE3), or CodonPlus (DE3)
genes cct1-8
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
genes CCT1-8, recombinant expression of GFP-tagged subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta in insect cells, method overview. Examination if recombinant hTRiC and or hTRiC-GFP are assembled into the correct and evolutionarily conserved subunit arrangement using disuccinimidyl suberate (DSS) XL-MS
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
genes cct1-8, recombinant overexpression of Strep-tagged wild-type and mutant CCT complexes in Escherichia coli strain BL21 Star(DE3)pRARE
-
genes CCT1-CCT8, recombinant expression of N-terminally FLAG-tagged proteins
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
genes encoding subunits CCT-alpha, CCT-beta, CCT-gamma, CCT-delta, CCT-epsilon, CCT-zeta-1, CCT-eta, and CCT-theta, DNA and amino acid sequence determination, sequences comparisons, quantitative real-time PCR expression analysis at different temperatures, overview. GaTRiC subunits are constitutively expressed at all temperatures with the exception of GaTRiCbeta subunit at 20°C reaching 4.5fold expression compared to optimal growth at 12°C
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
quantitative real-time reverse transcription-PCR expression analysis
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
recombinant ectopic overexpression in in Plasmodium falciparum of each of the N-terminally GFP-tagged PfTRiC subunits, under the expression of the strong, constitutively active HSP86 promoter, the subunits are additionally C-terminally tagged with a ten amino acid flexible linker sequence (PRPGAAHYAA) between the TRiC C-terminus and GFP to avoid disruption of heterohexadecamer formation. All GFP-tagged subunits are successfully overexpressed, except the PfTRiC-zeta subunit, where the GFP signal gets lost
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
recombinant enzyme MmCpn is expressed in pET21a-containing Escherichia coli strain Rosetta (DE3) pLys
-
recombinant expression of archaeal group II chaperonin Mm-cpn in Escherichia coli strain TAB21 lacking its group I chaperonin GroEL, and wild-type and mutant enzymes overexpression in Escherichia coli strain BL21(DE3)
recombinant expression of enzyme CPN in Escherichia coli strain BLR(DE3)/pET23a
-
recombinant expression of FLAG-tagged human TCP1, or CCT2- to CCT8-expressing plasmids in HEK-293T cells
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
recombinant expression of His-tagged TRiC with GFP-tagged CCT1 in High Five insect cells
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
recombinant expression of His-tagged wild-type and mutant enzyme oligomer rings in Escherichia coli
recombinant expression of LdTCP1epsilon subunit in Escherichia coli as His-tagged protein
A0A3Q8IJL9; E9BIZ7; K9ZSK4; A0A068B7V9; A0A3S7X5D6; R4QYR7; A0A3Q8IFF2; A0A3Q8II90
recombinant expression of wild-type and mutant enzymes in Escherichia coli strain BL21(DE3) RIL
subcloned into vector pET21a. The constructed pET21a-ApCpnB is transformed into Escherichia coli BL21 Codonplus (DE3)
-
the chaperonin gene PhCpn is amplified by PCR from the genomic DNA, subcloned into pET21a vector, and expressed in three Escherichia coli host cells such as BL21, Rosetta, and Codonplus (DE3)DE3. Among these host cells, Escherichia coli Rosetta shows the highest expression level of recombinant PhCpn at induction with 1 mM isopropyl beta-D-thiogalactoside
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
cardiac-specific upregulation of CCT components under time restricted feeding (TRF)
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
no significant changes in mRNA levels for any of the TRiC/CCT complex components at any of the virus levels examined
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
possesses two chaperonins, cold-inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high temperatures, respectively
role of AKT in regulating TCP1 downstream of FGFR2, Akt inhibition results in downregulation of TCP1 protein as well as reduced levels of Akt and RPS6 phosphorylation
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
subunit CCT1 is transcriptionally modulated by the driver oncogene, phosphatidylinositide 3-kinases (PI3K)
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
the TCP1 subunit of TRiC is regulated by fibroblast growth factor receptor 2 (FGFR2), the induction of TCP1 by FGFR2 is inhibited by PD173074, i.e. N-[2-[[4-(diethylamino)butyl]amino-6-(3,5-dimethoxyphenyl)pyrido[2,3-d]pyrimidin-7-yl]-N'-(1,1-dimethylethyl)urea], an ATP-competitive inhibitor. FGFR2 signals through PI3K and Akt to regulate TCP1 expression
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
possesses two chaperonins, cold-inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high temperatures, respectively
possesses two chaperonins, cold-inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high temperatures, respectively
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
TRiC can refold denatured AML1-175 (DBD) and restore its DNA binding activity in vitro. The reconstructed the TRiC-AML1-175 complex is formed in the presence of Ni2+-gold nanoparticles capable of binding to the His-tag on AML1-175. While AML1-175 is folded by TRiC to achieve its native function, ATP hydrolysis does not suffice to trigger its release from the chaperonin
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
TRiC/CCT dysfunction leads to various clinical disorders, and displays the potential to serve as an effective marker and target for pharmacological intervention for various diseases
drug development
medicine
synthesis
-
ApCpnB has both foldase and holdase activities and can be used as a powerful molecular machinery for the production of recombinant proteins as soluble and active forms in Escherichia coli
drug development
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
development of small-molecule inhibitors of TRiC as potential antiviral therapeutics
drug development
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the enzyme is a target for the specific treatments of AML1-ETO-positive leukemia. AML1-ETO suppression by small interfering RNAs (siRNAs) supports normal myeloid differentiation of t(8,21)-positive leukemic cells which highlights AML1-ETO as a major clinical target to treat AML. Inhibition of HSP70/90, two major proteostasis regulators, has shown antileukemic effects in AML1-ETO positive cells. Moreover, the mammalian cytosolic chaperonin TRiC (or CCT) modulates the synthesis, folding and activity of AML1-ETO by direct association, primarily through its DNA-binding domain (AML1-175), and that HSP70 promotes this interaction
drug development
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
development of cell-based CCT inhibitors using peptide reagents and HSF1A, a benzyl-pyrazole-based small molecule
drug development
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
the TRiC/CCT complex is required for mammarenavirus multiplication and is an attractive candidate for the development of host directed antivirals against human-pathogenic mammarenaviruses. Host-directed antivirals have gained great interest as an antiviral strategy to counteract the rapid emergence of drug-resistant viruses
drug development
-
development of cell-based CCT inhibitors using peptide reagents and HSF1A, a benzyl-pyrazole-based small molecule
-
medicine
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
subunit CCT2 is a chemotherapeutic target in uterine cancer
medicine
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
TRiC is a therapeutic target in breast cancer
medicine
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
TRiC/CCT can be a therapeutic target
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Shin, E.J.; Lee, J.W.; Kim, J.H.; Jeon, S.J.; Kim, Y.H.; Nam, S.W.
Overexpression, purification, and characterization of beta-subunit group II chaperonin from hyperthermophilic Aeropyrum pernix K1
J. Microbiol. Biotechnol.
20
542-549
2010
Aeropyrum pernix K1
brenda
Yan, Z.; Fujiwara, S.; Kohda, K.; Takagi, M.; Imanaka, T.
In vitro stabilization and in vivo solubilization of foreign proteins by the beta subunit of a chaperonin from the hyperthermophilic archaeon Pyrococcus sp. strain KOD1
Appl. Environ. Microbiol.
63
785-789
1997
Thermococcus kodakarensis (Q52500)
brenda
Okochi, M.; Matsuzaki, H.; Nomura, T.; Ishii, N.; Yohda, M.
Molecular characterization of the group II chaperonin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3
Extremophiles
9
127-134
2004
Pyrococcus horikoshii (O57762), Pyrococcus horikoshii OT-3 (O57762)
brenda
Franzetti, B.; Schoehn, G.; Ebel, C.; Gagnon, J.; Ruigrok, R.W.; Zaccai, G.
Characterization of a novel complex from halophilic archaebacteria, which displays chaperone-like activities in vitro
J. Biol. Chem.
276
29906-29914
2001
Haloarcula marismortui
brenda
Kim, J.H.; Lee, J.W.; Shin, E.J.; Nam, S.W.
Cooperativity of alpha- and beta-subunits of group II chaperonin from the hyperthermophilic archaeum Aeropyrum pernix K1
J. Microbiol. Biotechnol.
21
212-217
2011
Aeropyrum pernix (Q9YDK6 and Q9YA66), Aeropyrum pernix, Aeropyrum pernix DSM 11879 (Q9YDK6 and Q9YA66)
brenda
Lee, J.W.; Kim, S.W.; Kim, J.H.; Jeon, S.J.; Kwon, H.J.; Kim, B.W.; Nam, S.W.
Functional characterization of the alpha- and beta-subunits of a group II chaperonin from Aeropyrum pernix K1
J. Microbiol. Biotechnol.
23
818-825
2013
Aeropyrum pernix (Q9YDK6 and Q9YA66), Aeropyrum pernix (Q9YDK6), Aeropyrum pernix (Q9YA66), Aeropyrum pernix DSM 11879 (Q9YDK6 and Q9YA66)
brenda
Gao, L.; Danno, A.; Fujii, S.; Fukuda, W.; Imanaka, T.; Fujiwara, S.
Indole-3-glycerol-phosphate synthase is recognized by a cold-inducible group II chaperonin in Thermococcus kodakarensis
Appl. Environ. Microbiol.
78
3806-3815
2012
Thermococcus kodakarensis (Q52500), Thermococcus kodakarensis (P61111)
brenda
Jayasinghe, M.; Shrestha, P.; Wu, X.; Tehver, R.; Stan, G.
Weak intra-ring allosteric communications of the archaeal chaperonin thermosome revealed by normal mode analysis
Biophys. J.
103
1285-1295
2012
Thermoplasma acidophilum (P48424), Thermoplasma acidophilum (P48425), Thermoplasma acidophilum ATCC 25905 (P48424), Thermoplasma acidophilum ATCC 25905 (P48425)
brenda
Cong, Y.; Schroeder, G.; Meyer, A.; Jakana, J.; Ma, B.; Dougherty, M.; Schmid, M.; Reissmann, S.; Levitt, M.; Ludtke, S.; Frydman, J.; Chiu, W.
Symmetry-free cryo-EM structures of the chaperonin TRiC along its ATPase-driven conformational cycle
EMBO J.
31
720-730
2012
Bos taurus
brenda
Skjaerven, L.; Cuellar, J.; Martinez, A.; Valpuesta, J.M.
Dynamics, flexibility, and allostery in molecular chaperonins
FEBS Lett.
589
2522-2532
2015
Methanococcus maripaludis (Q877G8), Saccharomyces cerevisiae (P12612), Thermoplasma acidophilum (P48424), Thermoplasma acidophilum (P48425), Bos taurus (Q32L40), Saccharomyces cerevisiae ATCC 204508 (P12612), Thermoplasma acidophilum ATCC 25905 (P48424), Thermoplasma acidophilum ATCC 25905 (P48425)
brenda
Gao, L.; Imanaka, T.; Fujiwara, S.
A mutant chaperonin that is functional at lower temperatures enables hyperthermophilic Archaea to grow under cold-stress conditions
J. Bacteriol.
197
2642-2652
2015
Thermococcus kodakarensis (Q52500), Thermococcus kodakarensis (P61111), Thermococcus kodakarensis KU216 (Q52500)
brenda
Hongo, K.; Itai, H.; Mizobata, T.; Kawata, Y.
Varied effects of Pyrococcus furiosus prefoldin and P. furiosus chaperonin on the refolding reactions of substrate proteins
J. Biochem.
151
383-390
2012
Pyrococcus furiosus
brenda
Yamamoto, Y.Y.; Abe, Y.; Moriya, K.; Arita, M.; Noguchi, K.; Ishii, N.; Sekiguchi, H.; Sasaki, Y.C.; Yohda, M.
Inter-ring communication is dispensable in the reaction cycle of group II chaperonins
J. Mol. Biol.
426
2667-2678
2014
Thermococcus sp. (O24730), Thermococcus sp. (P61112), Thermococcus sp. KS-1 (O24730), Thermococcus sp. KS1 (P61112)
brenda
Nakagawa, A.; Moriya, K.; Arita, M.; Yamamoto, Y.; Kitamura, K.; Ishiguro, N.; Kanzaki, T.; Oka, T.; Makabe, K.; Kuwajima, K.; Yohda, M.
Dissection of the ATP-dependent conformational change cycle of a group II chaperonin
J. Mol. Biol.
426
447-459
2014
Thermococcus sp. (O24730), Thermococcus sp. (P61112), Thermococcus sp. KS-1 (O24730), Thermococcus sp. KS-1 (P61112)
brenda
Lopez, T.; Dalton, K.; Frydman, J.
The mechanism and function of group II chaperonins
J. Mol. Biol.
427
2919-2930
2015
Thermoplasma acidophilum, Saccharomyces cerevisiae, Methanococcus maripaludis
brenda
Sekiguchi, H.; Nakagawa, A.; Moriya, K.; Makabe, K.; Ichiyanagi, K.; Nozawa, S.; Sato, T.; Adachi, S.; Kuwajima, K.; Yohda, M.; Sasaki, Y.C.
ATP dependent rotational motion of group II chaperonin observed by X-ray single molecule tracking
PLoS ONE
8
e64176
2013
Thermococcus sp. (O24730), Thermococcus sp. (P61112), Thermococcus sp. KS-1 (O24730), Thermococcus sp. KS-1 (P61112)
brenda
Kim, J.; Shin, E.; Jeon, S.; Kim, Y.; Kim, P.; Lee, C.; Nam, S.
Overexpression, purification, and functional characterization of the group II chaperonin from the hyperthermophilic archaeum Pyrococcus horikoshii OT3
Biotechnol. Bioprocess Eng.
14
551-558
2009
Pyrococcus horikoshii (O57762)
-
brenda
Willison, K.R.
The structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring
Biochem. J.
475
3009-3034
2018
Arabidopsis thaliana (P28769 AND Q940P8 AND Q84WV1 AND Q9LV21 AND O04450 AND Q9M888 AND Q9SF16 AND Q94K05), Bos taurus (Q32L40 AND Q3ZBH0 AND Q3T0K2 AND F1N0E5 AND F1MWD3 AND Q3MHL7 AND Q2NKZ1 AND Q3ZCI9), Caenorhabditis elegans (P41988 AND P47207 AND Q9N4J8 AND P47208 AND P47209 AND P46550 AND Q9TZS5 AND Q9N358), Candida albicans (Q59QB7 AND Q59YC4 AND Q5AK16 AND Q59Z12 AND A0A1D8PMN9 AND Q59YH4 AND P47828), Candida albicans ATCC MYA-2876 (Q59QB7 AND Q59YC4 AND Q5AK16 AND Q59Z12 AND A0A1D8PMN9 AND Q59YH4 AND P47828), Danio rerio (Q9PW76 AND Q6PBW6 AND Q7T2P2 AND Q6P123 AND Q6NVI6 AND E9QGU4 AND B3DKJ0 AND A0A0R4IJT8), Dictyostelium discoideum (Q55BM4 AND Q54ES9 AND Q54TH8 AND Q54CL2 AND Q54TD3 AND Q76NU3 AND Q54ER7 AND Q552J0), Drosophila melanogaster (P12613 AND Q9W392 AND P48605 AND Q9VK69 AND Q7KKI0 AND Q9VXQ5 AND Q9VHL2 AND Q7K3J0), Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990), Mus musculus (P11983 AND P80314 AND P80318 AND P80315 AND P80316 AND P80317 AND P80313 AND P42932), Plasmodium falciparum (Q8II43 AND O97247 AND Q8I5C4 AND C0H5I7 AND O97282 AND C6KST5 AND O77323 AND O96220), Rattus norvegicus (P28480 AND Q5XIM9 AND Q6P502 AND Q7TPB1 AND Q68FQ0 AND Q3MHS9 AND D4AC23 AND D4ACB8), Rattus norvegicus Sprague-Dawley (P28480 AND Q5XIM9 AND Q6P502 AND Q7TPB1 AND Q68FQ0 AND Q3MHS9 AND D4AC23 AND D4ACB8), Saccharomyces cerevisiae (P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079), Saccharomyces cerevisiae ATCC 204508 (P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079)
brenda
Korobko, I.; Nadler-Holly, M.; Horovitz, A.
Transient kinetic analysis of ATP hydrolysis by the CCT/TRiC chaperonin
J. Mol. Biol.
428
4520-4527
2016
Saccharomyces cerevisiae (P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079), Saccharomyces cerevisiae ATCC 204508 (P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079)
brenda
Araki, K.; Suenaga, A.; Kusano, H.; Tanaka, R.; Hatta, T.; Natsume, T.; Fukui, K.
Functional profiling of asymmetrically-organized human CCT/TRiC chaperonin
Biochem. Biophys. Res. Commun.
481
232-238
2016
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990), Homo sapiens
brenda
Roh, S.H.; Kasembeli, M.M.; Galaz-Montoya, J.G.; Chiu, W.; Tweardy, D.J.
Chaperonin TRiC/CCT recognizes fusion oncoprotein AML1-ETO through subunit-specific interactions
Biophys. J.
110
2377-2385
2016
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
brenda
Balchin, D.; Milicic, G.; Strauss, M.; Hayer-Hartl, M.; Hartl, F.U.
Pathway of actin folding directed by the eukaryotic chaperonin TRiC
Cell
174
1507-1521.e16
2018
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
brenda
Gestaut, D.; Roh, S.H.; Ma, B.; Pintilie, G.; Joachimiak, L.A.; Leitner, A.; Walzthoeni, T.; Aebersold, R.; Chiu, W.; Frydman, J.
The chaperonin TRiC/CCT associates with prefoldin through a conserved electrostatic interface essential for cellular proteostasis
Cell
177
751-765.e15
2019
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
brenda
Berger, J.; Berger, S.; Li, M.; Jacoby, A.S.; Arner, A.; Bavi, N.; Stewart, A.G.; Currie, P.D.
In vivo function of the chaperonin TRiC in beta-actin folding during sarcomere assembly
Cell Rep.
22
313-322
2018
Danio rerio (Q9PW76 AND Q6PBW6 AND Q7T2P2 AND Q6P123 AND Q6NVI6 AND E9QGU4 AND B3DKJ0 AND A0A0R4IJT8)
brenda
Yusof, N.A.; Kamaruddin, S.; Abu Bakar, F.D.; Mahadi, N.M.; Abdul Murad, A.M.
Structural and functional insights into TRiC chaperonin from a psychrophilic yeast, Glaciozyma antarctica
Cell Stress Chaperones
24
351-368
2019
Glaciozyma antarctica (A0A1S6LQX4 AND A0A1S6LQU3 AND A0A1S6LQU0 AND A0A1S6LQU6 AND A0A1S6LQU1 AND A0A1S6LQU9 AND A0A1S6LQW6 AND A0A1S6LQW7), Glaciozyma antarctica
brenda
Spillman, N.J.; Beck, J.R.; Ganesan, S.M.; Niles, J.C.; Goldberg, D.E.
The chaperonin TRiC forms an oligomeric complex in the malaria parasite cytosol
Cell. Microbiol.
19
e12719
2017
Plasmodium falciparum (Q8II43 AND O97247 AND Q8I5C4 AND C0H5I7 AND O97282 AND C6KST5 AND O77323 AND O96220), Plasmodium falciparum, Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
brenda
Guest, S.T.; Kratche, Z.R.; Bollig-Fischer, A.; Haddad, R.; Ethier, S.P.
Two members of the TRiC chaperonin complex, CCT2 and TCP1 are essential for survival of breast cancer cells and are linked to driving oncogenes
Exp. Cell Res.
332
223-235
2015
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990), Homo sapiens
brenda
Melkani, G.C.; Bhide, S.; Han, A.; Vyas, J.; Livelo, C.; Bodmer, R.; Bernstein, S.I.
TRiC/CCT chaperonins are essential for maintaining myofibril organization, cardiac physiological rhythm, and lifespan
FEBS Lett.
591
3447-3458
2017
Drosophila melanogaster (P12613 AND Q9W392 AND P48605 AND Q9VK69 AND Q7KKI0 AND Q9VXQ5 AND Q9VHL2 AND Q7K3J0)
brenda
Roh, S.H.; Kasembeli, M.; Bakthavatsalam, D.; Chiu, W.; Tweardy, D.J.
Contribution of the type II chaperonin, TRiC/CCT, to oncogenesis
Int. J. Mol. Sci.
16
26706-26720
2015
Bos taurus (Q32L40 AND Q3ZBH0 AND Q3T0K2 AND F1N0E5 AND F1MWD3 AND Q3MHL7 AND Q2NKZ1 AND Q3ZCI9), Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
brenda
Shah, R.; Large, A.T.; Ursinus, A.; Lin, B.; Gowrinathan, P.; Martin, J.; Lund, P.A.
Replacement of GroEL in Escherichia coli by the group II chaperonin from the archaeon Methanococcus maripaludis
J. Bacteriol.
198
2692-2700
2016
Methanococcus maripaludis (Q877G8)
brenda
Roh, S.H.; Kasembeli, M.; Galaz-Montoya, J.G.; Trnka, M.; Lau, W.C.; Burlingame, A.; Chiu, W.; Tweardy, D.J.
Chaperonin TRiC/CCT modulates the folding and activity of leukemogenic fusion oncoprotein AML1-ETO
J. Biol. Chem.
291
4732-4741
2016
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990), Bos taurus (Q32L40 AND Q3ZBH0 AND Q3T0K2 AND F1N0E5 AND F1MWD3 AND Q3MHL7 AND Q2NKZ1 AND Q3ZCI9)
brenda
Zako, T.; Sahlan, M.; Fujii, S.; Yamamoto, Y.Y.; Tai, P.T.; Sakai, K.; Maeda, M.; Yohda, M.
Contribution of the C-terminal region of a group II chaperonin to its interaction with prefoldin and substrate transfer
J. Mol. Biol.
428
2405-2417
2016
Thermococcus sp. JCM 11816 (P61112 AND O24730)
brenda
Kim, S.; Lee, D.; Lee, J.; Song, H.; Kim, H.J.; Kim, K.T.
Vaccinia-related kinase 2 controls the stability of the eukaryotic chaperonin TRiC/CCT by inhibiting the deubiquitinating enzyme USP25
Mol. Cell. Biol.
35
1754-1762
2015
Mus musculus (P11983 AND P80314 AND P80318 AND P80315 AND P80316 AND P80317 AND P80313 AND P42932)
brenda
Knowlton, J.J.; Fernandez de Castro, I.; Ashbrook, A.W.; Gestaut, D.R.; Zamora, P.F.; Bauer, J.A.; Forrest, J.C.; Frydman, J.; Risco, C.; Dermody, T.S.
The TRiC chaperonin controls reovirus replication through outer-capsid folding
Nat. Microbiol.
3
481-493
2018
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
brenda
Zang, Y.; Jin, M.; Wang, H.; Cui, Z.; Kong, L.; Liu, C.; Cong, Y.
Staggered ATP binding mechanism of eukaryotic chaperonin TRiC (CCT) revealed through high-resolution cryo-EM
Nat. Struct. Mol. Biol.
23
1083-1091
2016
Saccharomyces cerevisiae (P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079), Saccharomyces cerevisiae
brenda
Kim, A.R.; Choi, K.W.
TRiC/CCT chaperonins are essential for organ growth by interacting with insulin/TOR signaling in Drosophila
Oncogene
38
4739-4754
2019
Drosophila melanogaster (P12613 AND Q9W392 AND P48605 AND Q9VK69 AND Q7KKI0 AND Q9VXQ5 AND Q9VHL2 AND Q7K3J0)
brenda
Ohhara, Y.; Nakamura, A.; Kato, Y.; Yamakawa-Kobayashi, K.
Chaperonin TRiC/CCT supports mitotic exit and entry into endocycle in Drosophila
PLoS Genet.
15
e1008121
2019
Drosophila melanogaster (P12613 AND Q9W392 AND P48605 AND Q9VK69 AND Q7KKI0 AND Q9VXQ5 AND Q9VHL2 AND Q7K3J0), Drosophila melanogaster Oregon R (P12613 AND Q9W392 AND P48605 AND Q9VK69 AND Q7KKI0 AND Q9VXQ5 AND Q9VHL2 AND Q7K3J0)
brenda
Yamamoto, Y.Y.; Uno, Y.; Sha, E.; Ikegami, K.; Ishii, N.; Dohmae, N.; Sekiguchi, H.; Sasaki, Y.C.; Yohda, M.
Asymmetry in the function and dynamics of the cytosolic group II chaperonin CCT/TRiC
PLoS ONE
12
e0176054
2017
Thermochaetoides thermophila
brenda
Moparthi, S.B.; Carlsson, U.; Vincentelli, R.; Jonsson, B.H.; Hammarstroem, P.; Wenger, J.
Differential conformational modulations of MreB folding upon interactions with GroEL/ES and TRiC chaperonin components
Sci. Rep.
6
28386
2016
Bos taurus (Q32L40 AND Q3ZBH0 AND Q3T0K2 AND F1N0E5 AND F1MWD3 AND Q3MHL7 AND Q2NKZ1 AND Q3ZCI9)
brenda
Smith, T.M.; Willardson, B.M.
Mechanistic insights into protein folding by the eukaryotic chaperonin complex CCT
Biochem. Soc. Trans.
50
1403-1414
2022
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990), Saccharomyces cerevisiae (P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079), Saccharomyces cerevisiae ATCC 204508 (P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079)
brenda
Cuellar, J.; Ludlam, W.G.; Tensmeyer, N.C.; Aoba, T.; Dhavale, M.; Santiago, C.; Bueno-Carrasco, M.T.; Mann, M.J.; Plimpton, R.L.; Makaju, A.; Franklin, S.; Willardson, B.M.; Valpuesta, J.M.
Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly
Nat. Commun.
10
2865
2019
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
brenda
Chen, Y.; Chen, Y.; Liu, W.
Chaperonin containing TCP1 subunit 6A may activate Notch and Wnt pathways to facilitate the malignant behaviors and cancer stemness in oral squamous cell carcinoma
Cancer Biol. Ther.
25
2287122
2024
Homo sapiens (P40227)
brenda
Gestaut, D.; Zhao, Y.; Park, J.; Ma, B.; Leitner, A.; Collier, M.; Pintilie, G.; Roh, S.H.; Chiu, W.; Frydman, J.
Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT
Cell
185
4770-4787.e20
2022
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
brenda
Zeng, C.; Han, S.; Pan, Y.; Huang, Z.; Zhang, B.; Zhang, B.
Revisiting the chaperonin T-complex protein-1 ring complex in human health and disease A proteostasis modulator and beyond
Clin. Transl. Med.
14
e1592
2024
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
brenda
Green, A.M.; DeWeerd, R.A.; OLeary, D.R.; Hansen, A.R.; Hayer, K.E.; Kulej, K.; Dineen, A.S.; Szeto, J.H.; Garcia, B.A.; Weitzman, M.D.
Interaction with the CCT chaperonin complex limits APOBEC3A cytidine deaminase cytotoxicity
EMBO Rep.
22
e52145
2021
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
brenda
Tang, W.S.; Cen, X.; Yao, S.S.; Yin, S.T.; Weng, L.; Zhao, T.J.; Wang, X.
TRiC/CCT chaperonin is required for the folding and inhibitory effect of WDTC1 on adipogenesis
Front. Cell Dev. Biol.
11
1225628
2023
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990), Mus musculus (P11983 AND P80314 AND P80318 AND P80315 AND P80316 AND P80317 AND P80313 AND P42932)
brenda
Wilkinson, M.D.; Ferreira, J.L.; Beeby, M.; Baum, J.; Willison, K.R.
The malaria parasite chaperonin containing TCP-1 (CCT) complex data integration with other CCT proteomes
Front. Mol. Biosci.
9
1057232
2022
Plasmodium falciparum (Q8II43 AND O97247 AND Q8I5C4 AND C0H5I7 AND O97282 AND C6KST5 AND O77323 AND O96220)
brenda
Anand, A.; Gautam, G.; Yadav, S.; Ramalingam, K.; Kumar Haldar, A.; Goyal, N.
Epsilon subunit of T-complex protein-1 from Leishmania donovani a tetrameric chaperonin
Gene
926
148637
2024
Leishmania donovani (A0A3Q8IJL9 AND E9BIZ7 AND K9ZSK4 AND A0A068B7V9 AND A0A3S7X5D6 AND R4QYR7 AND A0A3Q8IFF2 AND A0A3Q8II90), Leishmania donovani Dd8 (A0A3Q8IJL9 AND E9BIZ7 AND K9ZSK4 AND A0A068B7V9 AND A0A3S7X5D6 AND R4QYR7 AND A0A3Q8IFF2 AND A0A3Q8II90), Leishmania donovani MHOM/IN/80 (A0A3Q8IJL9 AND E9BIZ7 AND K9ZSK4 AND A0A068B7V9 AND A0A3S7X5D6 AND R4QYR7 AND A0A3Q8IFF2 AND A0A3Q8II90)
brenda
Sakabe, S.; Witwit, H.; Khafaji, R.; Cubitt, B.; de la Torre, J.C.
Chaperonin TRiC/CCT participates in mammarenavirus multiplication in human cells via interaction with the viral nucleoprotein
J. Virol.
97
e0168822
2023
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
brenda
Vetter, J.; Papa, G.; Tobler, K.; Rodriguez, J.M.; Kley, M.; Myers, M.; Wiesendanger, M.; Schraner, E.M.; Luque, D.; Burrone, O.R.; Fraefel, C.; Eichwald, C.
The recruitment of TRiC chaperonin in rotavirus viroplasms correlates with virus replication
mBio
15
e0049924
2024
Macaca mulatta (F6T521 AND F6PJP5 AND G7MDZ6 AND A0A5F7ZBU8 AND A0A1D5Q8I4 AND I0FKJ8 AND A0A1D5RDC8 AND A0A5F7Z7P5)
brenda
Kim, H.; Park, J.; Roh, S.H.
The structural basis of eukaryotic chaperonin TRiC/CCT action and folding
Mol. Cells
47
100012
2024
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990), Saccharomyces cerevisiae (P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079), Saccharomyces cerevisiae ATCC 204508 (P12612 AND P39076 AND P39077 AND P39078 AND P40413 AND P39079 AND P42943 AND P47079)
brenda
Zhao, Y.; Schmid, M.F.; Frydman, J.; Chiu, W.
CryoEM reveals the stochastic nature of individual ATP binding events in a group II chaperonin
Nat. Commun.
12
4754
2021
Methanococcus maripaludis
brenda
Park, J.; Kim, H.; Gestaut, D.; Lim, S.; Opoku-Nsiah, K.A.; Leitner, A.; Frydman, J.; Roh, S.H.
A structural vista of phosducin-like PhLP2A-chaperonin TRiC cooperation during the ATP-driven folding cycle
Nat. Commun.
15
1007
2024
Homo sapiens (P17987 AND P78371 AND P49368 AND P50991 AND P48643 AND P40227 AND Q99832 AND P50990)
brenda
EXTERNAL LINKS (specific for EC-Number 3.6.4.B10)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
