DC Field | Value | Language |
---|---|---|
dc.contributor.author | Park, Soyeon | ko |
dc.contributor.author | Li, Xueming | ko |
dc.contributor.author | Kim, Ho Min | ko |
dc.contributor.author | Singh, Chingakham Ranjit | ko |
dc.contributor.author | Tian, Geng | ko |
dc.contributor.author | Hoyt, Martin A. | ko |
dc.contributor.author | Lovell, Scott | ko |
dc.contributor.author | Battaile, Kevin P. | ko |
dc.contributor.author | Zolkiewski, Michal | ko |
dc.contributor.author | Coffino, Philip | ko |
dc.contributor.author | Roelofs, Jeroen | ko |
dc.contributor.author | Cheng, Yifan | ko |
dc.contributor.author | Finley, Daniel | ko |
dc.date.accessioned | 2019-04-15T15:31:16Z | - |
dc.date.available | 2019-04-15T15:31:16Z | - |
dc.date.created | 2013-05-31 | - |
dc.date.created | 2013-05-31 | - |
dc.date.created | 2013-05-31 | - |
dc.date.issued | 2013-05 | - |
dc.identifier.citation | NATURE, v.497, no.7450, pp.512 - 516 | - |
dc.identifier.issn | 0028-0836 | - |
dc.identifier.uri | http://hdl.handle.net/10203/255023 | - |
dc.description.abstract | The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric alpha-ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt carboxy-terminal tails inserting into pockets of the alpha-ring(1-4). Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit(5-10). Here we report that the base subassembly of the Saccharomyces cerevisiae proteasome, which includes the Rpt ring, forms a high-affinity complex with the CP. This complex is subject to active dissociation by the chaperones Hsm3, Nas6 and Rpn14. Chaperone-mediated dissociation was abrogated by a non-hydrolysable ATP analogue, indicating that chaperone action is coupled to nucleotide hydrolysis by the Rpt ring. Unexpectedly, synthetic Rpt tail peptides bound alpha-pockets with poor specificity, except for Rpt6, which uniquely bound the alpha 2/alpha 3-pocket. Although the Rpt6 tail is not visualized within an alpha-pocket in mature proteasomes(2-4), it inserts into the alpha 2/alpha 3-pocket in the base-CP complex and is important for complex formation. Thus, the Rpt-CP interface is reconfigured when the lid complex joins the nascent proteasome to form the mature holoenzyme. | - |
dc.language | English | - |
dc.publisher | NATURE PUBLISHING GROUP | - |
dc.title | Reconfiguration of the proteasome during chaperone-mediated assembly | - |
dc.type | Article | - |
dc.identifier.wosid | 000319254000053 | - |
dc.identifier.scopusid | 2-s2.0-84878131964 | - |
dc.type.rims | ART | - |
dc.citation.volume | 497 | - |
dc.citation.issue | 7450 | - |
dc.citation.beginningpage | 512 | - |
dc.citation.endingpage | 516 | - |
dc.citation.publicationname | NATURE | - |
dc.identifier.doi | 10.1038/nature12123 | - |
dc.contributor.localauthor | Kim, Ho Min | - |
dc.contributor.nonIdAuthor | Park, Soyeon | - |
dc.contributor.nonIdAuthor | Li, Xueming | - |
dc.contributor.nonIdAuthor | Singh, Chingakham Ranjit | - |
dc.contributor.nonIdAuthor | Tian, Geng | - |
dc.contributor.nonIdAuthor | Hoyt, Martin A. | - |
dc.contributor.nonIdAuthor | Lovell, Scott | - |
dc.contributor.nonIdAuthor | Battaile, Kevin P. | - |
dc.contributor.nonIdAuthor | Zolkiewski, Michal | - |
dc.contributor.nonIdAuthor | Coffino, Philip | - |
dc.contributor.nonIdAuthor | Roelofs, Jeroen | - |
dc.contributor.nonIdAuthor | Cheng, Yifan | - |
dc.contributor.nonIdAuthor | Finley, Daniel | - |
dc.type.journalArticle | Article | - |
dc.subject.keywordPlus | YEAST 26S PROTEASOME | - |
dc.subject.keywordPlus | REGULATORY PARTICLE | - |
dc.subject.keywordPlus | STRUCTURAL BASIS | - |
dc.subject.keywordPlus | 20S PROTEASOMES | - |
dc.subject.keywordPlus | S PROTEASOME | - |
dc.subject.keywordPlus | ATPASES | - |
dc.subject.keywordPlus | SUBUNIT | - |
dc.subject.keywordPlus | PATHWAY | - |
dc.subject.keywordPlus | CORE | - |
dc.subject.keywordPlus | GATE | - |
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