dc.contributor.author | Park, Soyeon | en_US |
dc.contributor.author | Li, Xueming | en_US |
dc.contributor.author | Kim, Ho Min | en_US |
dc.contributor.author | Singh, Chingakham Ranjit | en_US |
dc.contributor.author | Tian, Geng | en_US |
dc.contributor.author | Hoyt, Martin A. | en_US |
dc.contributor.author | Lovell, Scott | en_US |
dc.contributor.author | Battaile, Kevin P. | en_US |
dc.contributor.author | Zolkiewski, Michal | en_US |
dc.contributor.author | Coffino, Philip | en_US |
dc.contributor.author | Roelofs, Jeroen | en_US |
dc.contributor.author | Cheng, Yifan | en_US |
dc.contributor.author | Finley, Daniel | en_US |
dc.date.accessioned | 2014-03-11T02:49:35Z | |
dc.date.issued | 2013 | en_US |
dc.identifier.citation | Park, S., X. Li, H. M. Kim, C. R. Singh, G. Tian, M. A. Hoyt, S. Lovell, et al. 2013. “Reconfiguration of the proteasome during chaperone-mediated assembly.” Nature 497 (7450): 10.1038/nature12123. doi:10.1038/nature12123. http://dx.doi.org/10.1038/nature12123. | en |
dc.identifier.issn | 0028-0836 | en |
dc.identifier.uri | http://nrs.harvard.edu/urn-3:HUL.InstRepos:11879146 | |
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 |
dc.language.iso | en_US | en |
dc.relation.isversionof | doi:10.1038/nature12123 | en |
dc.relation.hasversion | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3687086/pdf/ | en |
dash.license | LAA | en_US |
dc.subject | proteasome | en |
dc.subject | chaperone | en |
dc.subject | single particle cryoEM | en |
dc.subject | ATPase | en |
dc.title | Reconfiguration of the proteasome during chaperone-mediated assembly | en |
dc.type | Journal Article | en_US |
dc.description.version | Version of Record | en |
dc.relation.journal | Nature | en |
dash.depositing.author | Tian, Geng | en_US |
dc.date.available | 2014-03-11T02:49:35Z | |
dc.identifier.doi | 10.1038/nature12123 | * |
dash.authorsordered | false | |
dash.contributor.affiliated | Tian, Geng | |
dash.contributor.affiliated | Finley, Daniel | |