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Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Gestaut, Daniel | - |
dc.contributor.author | Zhao, Yanyan | - |
dc.contributor.author | Park, Junsun | - |
dc.contributor.author | Ma, Boxue | - |
dc.contributor.author | Leitner, Alexander | - |
dc.contributor.author | Collier, Miranda | - |
dc.contributor.author | Pintilie, Grigore | - |
dc.contributor.author | Roh, Soung-Hun | - |
dc.contributor.author | Chiu, Wah | - |
dc.contributor.author | Frydman, Judith | - |
dc.date.accessioned | 2024-05-16T01:50:09Z | - |
dc.date.available | 2024-05-16T01:50:09Z | - |
dc.date.created | 2022-12-27 | - |
dc.date.created | 2022-12-27 | - |
dc.date.created | 2022-12-27 | - |
dc.date.issued | 2022-12 | - |
dc.identifier.citation | Cell, Vol.185 No.25, pp.4770-4787.e20 | - |
dc.identifier.issn | 0092-8674 | - |
dc.identifier.uri | https://hdl.handle.net/10371/202902 | - |
dc.description.abstract | © 2022 Elsevier Inc.The ATP-dependent ring-shaped chaperonin TRiC/CCT is essential for cellular proteostasis. To uncover why some eukaryotic proteins can only fold with TRiC assistance, we reconstituted the folding of β-tubulin using human prefoldin and TRiC. We find unstructured β-tubulin is delivered by prefoldin to the open TRiC chamber followed by ATP-dependent chamber closure. Cryo-EM resolves four near-atomic-resolution structures containing progressively folded β-tubulin intermediates within the closed TRiC chamber, culminating in native tubulin. This substrate folding pathway appears closely guided by site-specific interactions with conserved regions in the TRiC chamber. Initial electrostatic interactions between the TRiC interior wall and both the folded tubulin N domain and its C-terminal E-hook tail establish the native substrate topology, thus enabling C-domain folding. Intrinsically disordered CCT C termini within the chamber promote subsequent folding of tubulin's core and middle domains and GTP-binding. Thus, TRiC's chamber provides chemical and topological directives that shape the folding landscape of its obligate substrates. | - |
dc.language | 영어 | - |
dc.publisher | Cell Press | - |
dc.title | Structural visualization of the tubulin folding pathway directed by human chaperonin TRiC/CCT | - |
dc.type | Article | - |
dc.identifier.doi | 10.1016/j.cell.2022.11.014 | - |
dc.citation.journaltitle | Cell | - |
dc.identifier.wosid | 000900759000003 | - |
dc.identifier.scopusid | 2-s2.0-85143850049 | - |
dc.citation.endpage | 4787.e20 | - |
dc.citation.number | 25 | - |
dc.citation.startpage | 4770 | - |
dc.citation.volume | 185 | - |
dc.description.isOpenAccess | Y | - |
dc.contributor.affiliatedAuthor | Roh, Soung-Hun | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.subject.keywordPlus | CRYO-EM STRUCTURE | - |
dc.subject.keywordPlus | PROTEINS | - |
dc.subject.keywordPlus | FTSZ | - |
dc.subject.keywordPlus | MASS | - |
dc.subject.keywordPlus | BINDING | - |
dc.subject.keywordPlus | CONFORMATION | - |
dc.subject.keywordPlus | CYTOSKELETON | - |
dc.subject.keywordPlus | MECHANISMS | - |
dc.subject.keywordPlus | GROEL/ES | - |
dc.subject.keywordPlus | REVEALS | - |
dc.subject.keywordAuthor | chaperone | - |
dc.subject.keywordAuthor | chaperonin | - |
dc.subject.keywordAuthor | cryo-EM | - |
dc.subject.keywordAuthor | prefoldin | - |
dc.subject.keywordAuthor | TRiC/CCT | - |
dc.subject.keywordAuthor | tubulin | - |
dc.subject.keywordAuthor | XL-MS | - |
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