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• W1986245350 endingPage "17744" @default.
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• W1986245350 abstract "Chaperonins are a family of chaperones that encapsulate their substrates and assist their folding in an ATP-dependent manner. The ubiquitous eukaryotic chaperonin, TCP-1 ring complex (TRiC), is a hetero-oligomeric complex composed of two rings, each formed from eight different CCT (chaperonin containing TCP-1) subunits. Each CCT subunit may have distinct substrate recognition and ATP hydrolysis properties. We have expressed each human CCT subunit individually in Escherichia coli to investigate whether they form chaperonin-like double ring complexes. CCT4 and CCT5, but not the other six CCT subunits, formed high molecular weight complexes within the E. coli cells that sedimented about 20S in sucrose gradients. When CCT4 and CCT5 were purified, they were both organized as two back-to-back rings of eight subunits each, as seen by negative stain and cryo-electron microscopy. This morphology is consistent with that of the hetero-oligomeric double-ring TRiC purified from bovine testes and HeLa cells. Both CCT4 and CCT5 homo-oligomers hydrolyzed ATP at a rate similar to human TRiC and were active as assayed by luciferase refolding and human γD-crystallin aggregation suppression and refolding. Thus, both CCT4 and CCT5 homo-oligomers have the property of forming 8-fold double rings absent the other subunits, and these complexes carry out chaperonin reactions without other partner subunits.Background: The subunit-specific roles of the CCT subunits in the chaperonin, TRiC, have not been elucidated.Results: When expressed in E. coli, CCT4 and CCT5 form TRiC-like homo-oligomeric rings.Conclusion: TRiC does not require all eight CCT subunits to form functional rings.Significance: The unexpected formation of homo-oligomeric CCT rings provides clues into the assembly of TRiC as a complex. Chaperonins are a family of chaperones that encapsulate their substrates and assist their folding in an ATP-dependent manner. The ubiquitous eukaryotic chaperonin, TCP-1 ring complex (TRiC), is a hetero-oligomeric complex composed of two rings, each formed from eight different CCT (chaperonin containing TCP-1) subunits. Each CCT subunit may have distinct substrate recognition and ATP hydrolysis properties. We have expressed each human CCT subunit individually in Escherichia coli to investigate whether they form chaperonin-like double ring complexes. CCT4 and CCT5, but not the other six CCT subunits, formed high molecular weight complexes within the E. coli cells that sedimented about 20S in sucrose gradients. When CCT4 and CCT5 were purified, they were both organized as two back-to-back rings of eight subunits each, as seen by negative stain and cryo-electron microscopy. This morphology is consistent with that of the hetero-oligomeric double-ring TRiC purified from bovine testes and HeLa cells. Both CCT4 and CCT5 homo-oligomers hydrolyzed ATP at a rate similar to human TRiC and were active as assayed by luciferase refolding and human γD-crystallin aggregation suppression and refolding. Thus, both CCT4 and CCT5 homo-oligomers have the property of forming 8-fold double rings absent the other subunits, and these complexes carry out chaperonin reactions without other partner subunits. Background: The subunit-specific roles of the CCT subunits in the chaperonin, TRiC, have not been elucidated. Results: When expressed in E. coli, CCT4 and CCT5 form TRiC-like homo-oligomeric rings. Conclusion: TRiC does not require all eight CCT subunits to form functional rings. Significance: The unexpected formation of homo-oligomeric CCT rings provides clues into the assembly of TRiC as a complex." @default.
• W1986245350 created "2016-06-24" @default.
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• W1986245350 date "2013-06-01" @default.
• W1986245350 modified "2023-09-27" @default.
• W1986245350 title "Human CCT4 and CCT5 Chaperonin Subunits Expressed in Escherichia coli Form Biologically Active Homo-oligomers" @default.
• W1986245350 cites W1532878531 @default.
• W1986245350 cites W1558206554 @default.
• W1986245350 cites W1575788408 @default.
• W1986245350 cites W1783115640 @default.
• W1986245350 cites W1892996896 @default.
• W1986245350 cites W1965187701 @default.
• W1986245350 cites W1965621240 @default.
• W1986245350 cites W1971090714 @default.
• W1986245350 cites W1971108880 @default.
• W1986245350 cites W1974229917 @default.
• W1986245350 cites W1975328921 @default.
• W1986245350 cites W1976129653 @default.
• W1986245350 cites W1976321372 @default.
• W1986245350 cites W1980166220 @default.
• W1986245350 cites W1985408089 @default.
• W1986245350 cites W1985876389 @default.
• W1986245350 cites W2000489361 @default.
• W1986245350 cites W2006340058 @default.
• W1986245350 cites W2009115466 @default.
• W1986245350 cites W2009651821 @default.
• W1986245350 cites W2014484295 @default.
• W1986245350 cites W2019842414 @default.
• W1986245350 cites W2021501314 @default.
• W1986245350 cites W2024277721 @default.
• W1986245350 cites W2030345298 @default.
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• W1986245350 cites W2078123480 @default.
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• W1986245350 doi "https://doi.org/10.1074/jbc.m112.443929" @default.
• W1986245350 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3682573" @default.
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