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dc.contributor.authorPark, Soyeon
dc.contributor.authorLi, Xueming
dc.contributor.authorKim, Ho Min
dc.contributor.authorSingh, Chingakham Ranjit
dc.contributor.authorTian, Geng
dc.contributor.authorHoyt, Martin A.
dc.contributor.authorLovell, Scott
dc.contributor.authorBattaile, Michal
dc.contributor.authorCoffino, Philip
dc.contributor.authorRoelofs, Jeroen
dc.contributor.authorCheng, Yifan
dc.contributor.authorFinley, Daniel
dc.identifier.citationPark, 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.
dc.description.abstractThe 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.publisherNature Publishing Groupen_US
dc.subjectSingle particle cryoEMen_US
dc.titleReconfiguration of the proteasome during chaperone-mediated assemblyen_US
kusw.kuauthorLovell, Scott
kusw.kudepartmentHiguchi Biosciences Centeren_US
kusw.oanotesPer SHERPA/RoMEO 4/27/2017: Author's Pre-print: green tick author can archive pre-print (ie pre-refereeing) Author's Post-print: grey tick subject to Restrictions below, author can archive post-print (ie final draft post-refereeing) Restrictions:

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Authors retain copyright Author's pre-print on arXiv or bioRXiv Author's post-print on author's personal website, institutional repository, PubMed Central or funding body's archive Published source must be acknowledged Must link to publisher version with DOI Publisher's version/PDF cannot be used
kusw.oaversionScholarly/refereed, author accepted manuscripten_US
kusw.oapolicyThis item meets KU Open Access policy criteria.en_US

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