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Reconfiguration of the proteasome during chaperone-mediated assembly
dc.contributor.author | Park, Soyeon | |
dc.contributor.author | Li, Xueming | |
dc.contributor.author | Kim, Ho Min | |
dc.contributor.author | Singh, Chingakham Ranjit | |
dc.contributor.author | Tian, Geng | |
dc.contributor.author | Hoyt, Martin A. | |
dc.contributor.author | Lovell, Scott | |
dc.contributor.author | Battaile, Michal | |
dc.contributor.author | Coffino, Philip | |
dc.contributor.author | Roelofs, Jeroen | |
dc.contributor.author | Cheng, Yifan | |
dc.contributor.author | Finley, Daniel | |
dc.date.accessioned | 2017-04-27T16:31:28Z | |
dc.date.available | 2017-04-27T16:31:28Z | |
dc.date.issued | 2013-05-23 | |
dc.identifier.citation | Park, S., Li, X., Kim, H. M., Singh, C. R., Tian, G., Hoyt, M. A., … Finley, D. (2013). Reconfiguration of the proteasome during chaperone-mediated assembly. Nature, 497(7450), 512–516. http://doi.org/10.1038/nature12123 | en_US |
dc.identifier.uri | http://hdl.handle.net/1808/23830 | |
dc.description.abstract | The proteasomal ATPase ring, comprising Rpt1-Rpt6, associates with the heptameric α ring of the proteasome core particle (CP) in the mature proteasome, with the Rpt C-terminal tails inserting into pockets of the α ring1–4. Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit5–10. We report that the base subassembly of the 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 nonhydrolyzable ATP analog, indicating that chaperone action is coupled to nucleotide hydrolysis by the Rpt ring. Unexpectedly, synthetic Rpt tail peptides bound α pockets with poor specificity, except for Rpt6, which uniquely bound the α2/α3 pocket. Although the Rpt6 tail is not visualized within an α pocket in mature proteasomes2–4, it inserts into the α2/α3 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. | en_US |
dc.publisher | Nature Publishing Group | en_US |
dc.subject | Proteasome | en_US |
dc.subject | Chaperone | en_US |
dc.subject | Single particle cryoEM | en_US |
dc.subject | ATPase | en_US |
dc.title | Reconfiguration of the proteasome during chaperone-mediated assembly | en_US |
dc.type | Article | en_US |
kusw.kuauthor | Lovell, Scott | |
kusw.kudepartment | Higuchi Biosciences Center | en_US |
dc.identifier.doi | 10.1038/nature12123 | en_US |
kusw.oaversion | Scholarly/refereed, author accepted manuscript | en_US |
kusw.oapolicy | This item meets KU Open Access policy criteria. | en_US |
dc.identifier.pmid | PMC3687086 | en_US |
dc.rights.accessrights | openAccess |