3.6.4.B10: chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)
This is an abbreviated version!
For detailed information about chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing), go to the full flat file.
Word Map on EC 3.6.4.B10
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3.6.4.B10
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chaperonins
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tubulins
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actin
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hetero-oligomeric
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cytoskeletal
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groel
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prefoldin
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chaperonin-containing
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huntingtin
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proteostasis
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double-ring
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tailless
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polyglutamine
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polyq
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inter-ring
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phosducin-like
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synthesis
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back-to-back
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drug development
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protein-folding
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homo-oligomeric
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acidophilum
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beta-tubulin
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thermoplasma
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medicine
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cryo-electron
- 3.6.4.B10
- chaperonins
- tubulins
- actin
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hetero-oligomeric
- cytoskeletal
- groel
- prefoldin
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chaperonin-containing
- huntingtin
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proteostasis
-
double-ring
-
tailless
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polyglutamine
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polyq
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inter-ring
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phosducin-like
- synthesis
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back-to-back
- drug development
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protein-folding
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homo-oligomeric
- acidophilum
- beta-tubulin
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thermoplasma
- medicine
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cryo-electron
Reaction
Synonyms
alpha/beta-thermosome, ApCpnB, archaeal chaperonin, CCT, CCT ATPase, CCT chaperonin, CCT complex, CCT/TRiC, CCT/TRiC chaperonin, CCT/TRiC complex, CCT2, chaperonin B, chaperonin containing t-complex polypeptide-1, chaperonin containing TCP-1, chaperonin containing TCP1, chaperonin TCP-1 ring complex, chaperonin TRiC, chaperonin TRiC/CCT, chaperonin-containing t-complex polypeptide 1, cPKA, CpkB, CtCCT, cytosolic chaperonin TRiC, eukaryotic chaperone complex, eukaryotic chaperonin, eukaryotic chaperonin TRiC, eukaryotic group II chaperonin, GaTRiC, group II chaperonin, group II chaperonin CCT/TRiC, group II CPN, HsTRiC, Mm-cpn, MmCpn, More, PfCPN, PfTRiC, PhCPN, Plasmodium TRiC, protein P45, T-complex polypeptide-1 ring complex, T-complex protein 1, T-complex protein 1 ring complex, T-complex protein-1 ring complex, TCP-1, TCP-1 ring complex, TCP1, TCP1 ring complex, thermosome, TKS1-CPN, TriC, TRiC chaperonin, TRiC chaperonin complex, TRiC/CCT, type II chaperonin
ECTree
3.6.4.B10 chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)Advanced search results
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results (Substrates Products
Substrates Products on EC 3.6.4.B10 - chaperonin ATPase (protein-folding, protecting from aggregation, protein stabilizing)
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ATP + H2O
ADP + phosphate
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
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-
?
ATP + H2O
ADP + phosphate
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
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-
?
ATP + H2O
ADP + phosphate
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
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-
?
ATP + H2O
ADP + phosphate
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
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-
?
ATP + H2O
ADP + phosphate
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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
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-
?
ATP + H2O
ADP + phosphate
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
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-
-
?
ATP + H2O
ADP + phosphate
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enzyme conformational changes upon ATP binding and throughout the ATPase cycle, structure-function relationship, overview
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-
?
ATP + H2O
ADP + phosphate
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
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-
-
?
ATP + H2O
ADP + phosphate
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
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-
-
?
ATP + H2O
ADP + phosphate
Q59QB7; Q59YC4; Q5AK16; Q59Z12; A0A1D8PMN9; Q59YH4; P47828
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-
-
?
ATP + H2O
ADP + phosphate
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
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-
-
?
ATP + H2O
ADP + phosphate
Q55BM4; Q54ES9; Q54TH8; Q54CL2; Q54TD3; Q76NU3; Q54ER7; Q552J0
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-
-
?
ATP + H2O
ADP + phosphate
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
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-
-
?
ATP + H2O
ADP + phosphate
A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
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-
-
?
ATP + H2O
ADP + phosphate
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the enzyme can protect halophilic proteins against denaturation under conditions of cellular hyposaline stress
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-
?
ATP + H2O
ADP + phosphate
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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
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-
?
ATP + H2O
ADP + phosphate
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
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-
-
?
ATP + H2O
ADP + phosphate
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nucleotide binding structure and conformational changes, overview
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-
?
ATP + H2O
ADP + phosphate
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
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-
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?
ATP + H2O
ADP + phosphate
Q8II43; O97247; Q8I5C4; C0H5I7; O97282; C6KST5; O77323; O96220
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-
-
?
ATP + H2O
ADP + phosphate
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
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?
ATP + H2O
ADP + phosphate
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
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?
ATP + H2O
ADP + phosphate
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
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?
ATP + H2O
ADP + phosphate
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
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-
-
?
ATP + H2O
ADP + phosphate
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
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-
-
?
ATP + H2O
ADP + phosphate
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nucleotide binding structure and conformational changes, overview
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-
?
ATP + H2O
ADP + phosphate
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
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?
ATP + H2O
ADP + phosphate
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nucleotide binding structure and conformational changes, overview
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-
?
CTP + H2O
CDP + phosphate
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
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-
?
CTP + H2O
CDP + phosphate
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
-
-
?
GTP + H2O
GDP + phosphate
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
-
-
?
GTP + H2O
GDP + phosphate
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
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-
?
UTP + H2O
UDP + phosphate
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
-
-
?
UTP + H2O
UDP + phosphate
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
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-
?
additional information
?
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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
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-
?
additional information
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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
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-
?
additional information
?
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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
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?
additional information
?
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Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
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
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additional information
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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 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
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additional information
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P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
the CCT complex physically interacts with TOR signaling components including TOR, Rheb, and S6K
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additional information
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A0A1S6LQX4; A0A1S6LQU3; A0A1S6LQU0; A0A1S6LQU6; A0A1S6LQU1; A0A1S6LQU9; A0A1S6LQW6; A0A1S6LQW7
GaTRiC acts a chaperonin mediating folding of denatured luciferase to the functional stage
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additional information
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GaTRiC acts a chaperonin mediating folding of denatured luciferase to the functional stage
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additional information
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P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
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
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additional information
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P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
TRiC binds to and modulates cancer related proteins
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additional information
?
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P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
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
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additional information
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P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
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
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additional information
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P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
reovirus sigma3 is a TRiC substrate
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additional information
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P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
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
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additional information
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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
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additional information
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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
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?
additional information
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P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
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
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additional information
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P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
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
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additional information
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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
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additional information
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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
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additional information
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P12612; P39076; P39077; P39078; P40413; P39079; P42943; P47079
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
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additional information
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Thermochaetoides thermophila
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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
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additional information
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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
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additional information
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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
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additional information
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indole-3-glycerol-phosphate synthase, TrpC, is a specific target protein of CpkA
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additional information
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indole-3-glycerol-phosphate synthase, TrpC, is a specific target protein of CpkA
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additional information
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indole-3-glycerol-phosphate synthase, TrpC, is no target protein for CpkB
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additional information
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indole-3-glycerol-phosphate synthase, TrpC, is no target protein for CpkB
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additional information
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ATP-dependent rotational motion of a group II chaperonin
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additional information
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ATP-dependent rotational motion of a group II chaperonin
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additional information
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enzyme TKS1-CPN shows a strong protein-folding activity
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additional information
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enzyme TKS1-CPN shows a strong protein-folding activity
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additional information
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the enzyme assists in folding of IPMDH
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additional information
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ATP-dependent rotational motion of a group II chaperonin
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additional information
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ATP-dependent rotational motion of a group II chaperonin
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additional information
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enzyme TKS1-CPN shows a strong protein-folding activity
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additional information
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enzyme TKS1-CPN shows a strong protein-folding activity
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