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A hierarchical assembly pathway directs the unique subunit arrangement of TRiC/CCT

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dc.contributor.authorBetancourt Moreira, Karen-
dc.contributor.authorCollier, Miranda P.-
dc.contributor.authorLeitner, Alexander-
dc.contributor.authorLi, Kathy H.-
dc.contributor.authorLachapel, Ivana L. Serrano-
dc.contributor.authorMcCarthy, Frank-
dc.contributor.authorOpoku-Nsiah, Kwadwo A.-
dc.contributor.authorMorales-Polanco, Fabián-
dc.contributor.authorBarbosa, Natália-
dc.contributor.authorGestaut, Daniel-
dc.contributor.authorSamant, Rahul S.-
dc.contributor.authorRoh, Soung-hun-
dc.contributor.authorFrydman, Judith-
dc.date.accessioned2024-05-16T01:49:39Z-
dc.date.available2024-05-16T01:49:39Z-
dc.date.created2023-09-07-
dc.date.created2023-09-07-
dc.date.issued2023-09-
dc.identifier.citationMolecular Cell, Vol.83 No.17, pp.3123-3139.e8-
dc.identifier.issn1097-2765-
dc.identifier.urihttps://hdl.handle.net/10371/202893-
dc.description.abstractHow the essential eukaryotic chaperonin TRiC/CCT assembles from eight distinct subunits into a unique double-ring architecture remains undefined. We show TRiC assembly involves a hierarchical pathway that segregates subunits with distinct functional properties until holocomplex (HC) completion. A stable, likely early intermediate arises from small oligomers containing CCT2, CCT4, CCT5, and CCT7, contiguous subunits that constitute the negatively charged hemisphere of the TRiC chamber, which has weak affinity for unfolded actin. The remaining subunits CCT8, CCT1, CCT3, and CCT6, which comprise the positively charged chamber hemisphere that binds unfolded actin more strongly, join the ring individually. Unincorporated late-assembling subunits are highly labile in cells, which prevents their accumulation and premature substrate binding. Recapitulation of assembly in a recombinant system demonstrates that the subunits in each hemisphere readily form stable, noncanonical TRiC-like HCs with aberrant functional properties. Thus, regulation of TRiC assembly along a biochemical axis disfavors the formation of stable alternative chaperonin complexes.-
dc.language영어-
dc.publisherCell Press-
dc.titleA hierarchical assembly pathway directs the unique subunit arrangement of TRiC/CCT-
dc.typeArticle-
dc.identifier.doi10.1016/j.molcel.2023.07.031-
dc.citation.journaltitleMolecular Cell-
dc.identifier.wosid001097421500001-
dc.identifier.scopusid2-s2.0-85169068721-
dc.citation.endpage3139.e8-
dc.citation.number17-
dc.citation.startpage3123-
dc.citation.volume83-
dc.description.isOpenAccessN-
dc.contributor.affiliatedAuthorRoh, Soung-hun-
dc.type.docTypeArticle-
dc.description.journalClass1-
dc.subject.keywordPlusCHAPERONIN CCT-
dc.subject.keywordPlusHEPATOCELLULAR-CARCINOMA-
dc.subject.keywordPlusMOLECULAR ARCHITECTURE-
dc.subject.keywordPlusCOMPUTATIONAL PLATFORM-
dc.subject.keywordPlusCELL-PROLIFERATION-
dc.subject.keywordPlusOVER-EXPRESSION-
dc.subject.keywordPlusCOMPLEX-
dc.subject.keywordPlusBIOGENESIS-
dc.subject.keywordPlusMECHANISM-
dc.subject.keywordPlusMASS-
dc.subject.keywordAuthoractin folding-
dc.subject.keywordAuthorassembly intermediates-
dc.subject.keywordAuthorchaperonin-
dc.subject.keywordAuthorcomplex assembly-
dc.subject.keywordAuthororphan subunits-
dc.subject.keywordAuthorprotein folding-
dc.subject.keywordAuthorTRiC/CCT-
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  • College of Natural Sciences
  • School of Biological Sciences
Research Area Cryogenic Electron Microscopy (Cryo-EM), Structural Biology, 분자생물학, 생물물리학, 생화학

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