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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
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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
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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
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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
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the enzyme belongs to the group II chaperonins
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
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
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
chaperonin TRiC is evolutionarily conserved
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
Thermochaetoides thermophila
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chaperonins are subdivided into two families, group I and group II chaperonins
evolution
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
co-evolution of CCT and the eukaryotic cytoskeleton, overview
evolution
P17987; P78371; P49368; P50991; P48643; P40227; Q99832; P50990
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
P11983; P80314; P80318; P80315; P80316; P80317; P80313; P42932
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
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
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
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
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
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
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
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the enzyme belongs to the group II chaperonins, that play important roles in protein homeostasis in the eukaryotic cytosol and in Archaea
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evolution
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chaperonin TRiC is evolutionarily conserved
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evolution
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co-evolution of CCT and the eukaryotic cytoskeleton, overview
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evolution
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co-evolution of CCT and the eukaryotic cytoskeleton, overview
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evolution
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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
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evolution
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co-evolution of CCT and the eukaryotic cytoskeleton, overview
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evolution
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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
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evolution
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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
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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
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
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
deletion of the phosducin III gene causes embryo division arrest with astral microtubule defects
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
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
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
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
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
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 TRiC in HEPG2 cells reduces their sensitivity to interleukin-6 induced STAT3 activation
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
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
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
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
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
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
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
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
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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
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malfunction
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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
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metabolism
Q32L40; Q3ZBH0; Q3T0K2; F1N0E5; F1MWD3; Q3MHL7; Q2NKZ1; Q3ZCI9
CCT-actin system, overview
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
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
CCT-actin system, overview
metabolism
Q9PW76; Q6PBW6; Q7T2P2; Q6P123; Q6NVI6; E9QGU4; B3DKJ0; A0A0R4IJT8
CCT-actin system, overview
metabolism
P28480; Q5XIM9; Q6P502; Q7TPB1; Q68FQ0; Q3MHS9; D4AC23; D4ACB8
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
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
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
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
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
-
CCT-actin system, overview
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metabolism
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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
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physiological function
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the enzyme can protect halophilic proteins against denaturation under conditions of cellular hyposaline stress
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 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 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
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
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
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
-
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
the CpkA C-terminal region plays a key role in cell growth at 60°C
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
P28769; Q940P8; Q84WV1; Q9LV21; O04450; Q9M888; Q9SF16; Q94K05
the enzyme complex CCT is involved in stem cell identity and protein translocation
physiological function
P41988; P47207; Q9N4J8; P47208; P47209; P46550; Q9TZS5; Q9N358
the enzyme is involved in invasion and lifespan extension
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
Thermochaetoides thermophila
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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
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
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
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
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
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
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
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
-
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
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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
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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
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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
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physiological function
-
CCT is a key modulator of echinocandin susceptibility
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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
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physiological function
-
subunit CCT8 and the CCT complex are involved in Ras signalling and morphogenesis, and in the polarisome and cell polarity, respectively
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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
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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
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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
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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
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additional information
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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
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
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
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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
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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
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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
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
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 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
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
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
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
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
P12613; Q9W392; P48605; Q9VK69; Q7KKI0; Q9VXQ5; Q9VHL2; Q7K3J0
all CCT subunits are required for the CCT complex function
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
ATP hydrolysis is important to attain the closed conformation of the enzyme
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
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
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
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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
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
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
individual subunits of TRiC have been shown to have protein-folding capacity
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
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Thermochaetoides thermophila
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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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
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
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reaction cycle model for group II chaperonins, ATP-binding, stopped-flow fluorometry and stopped-flow small-angle X-ray scattering, overview
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additional information
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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
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additional information
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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
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additional information
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structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview
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additional information
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possesses two chaperonins, cold-inducible CpkA and heat-inducible CpkB, which are involved in adaptation to low and high temperatures, respectively
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additional information
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structure and evolution of eukaryotic chaperonin-containing TCP-1 and its mechanism that folds actin into a protein spring, overview
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additional information
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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
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additional information
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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
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additional information
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determination of kinetic intermediates in the sequential allosteric pathway of CCT/TRiC, kinetic mechanism and model, overview
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additional information
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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
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additional information
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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
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additional information
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group II chaperonins cycle between an open, substrate-receptive conformation and a closed, substrate-trapping conformation, structure modeling, detailed overview
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additional information
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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
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