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Reconfiguration of the proteasome during chaperone-mediated assembly

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 ring(1–4). Rpt ring assembly is mediated by four chaperones, each binding a distinct R...

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Autores principales: Park, Soyeon, Li, Xueming, Kim, Ho Min, Singh, Chingakham Ranjit, Tian, Geng, Hoyt, Martin A., Lovell, Scott, Battaile, Kevin P., Zolkiewski, Michal, Coffino, Philip, Roelofs, Jeroen, Cheng, Yifan, Finley, Daniel
Formato: Online Artículo Texto
Lenguaje:English
Publicado: 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3687086/
https://www.ncbi.nlm.nih.gov/pubmed/23644457
http://dx.doi.org/10.1038/nature12123
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author Park, Soyeon
Li, Xueming
Kim, Ho Min
Singh, Chingakham Ranjit
Tian, Geng
Hoyt, Martin A.
Lovell, Scott
Battaile, Kevin P.
Zolkiewski, Michal
Coffino, Philip
Roelofs, Jeroen
Cheng, Yifan
Finley, Daniel
author_facet Park, Soyeon
Li, Xueming
Kim, Ho Min
Singh, Chingakham Ranjit
Tian, Geng
Hoyt, Martin A.
Lovell, Scott
Battaile, Kevin P.
Zolkiewski, Michal
Coffino, Philip
Roelofs, Jeroen
Cheng, Yifan
Finley, Daniel
author_sort Park, Soyeon
collection PubMed
description 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 ring(1–4). Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit(5–10). 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 proteasomes(2–4), 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.
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spelling pubmed-36870862013-11-23 Reconfiguration of the proteasome during chaperone-mediated assembly Park, Soyeon Li, Xueming Kim, Ho Min Singh, Chingakham Ranjit Tian, Geng Hoyt, Martin A. Lovell, Scott Battaile, Kevin P. Zolkiewski, Michal Coffino, Philip Roelofs, Jeroen Cheng, Yifan Finley, Daniel Nature Article 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 ring(1–4). Rpt ring assembly is mediated by four chaperones, each binding a distinct Rpt subunit(5–10). 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 proteasomes(2–4), 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. 2013-05-05 2013-05-23 /pmc/articles/PMC3687086/ /pubmed/23644457 http://dx.doi.org/10.1038/nature12123 Text en Users may view, print, copy, download and text and data- mine the content in such documents, for the purposes of academic research, subject always to the full Conditions of use: http://www.nature.com/authors/editorial_policies/license.html#terms
spellingShingle Article
Park, Soyeon
Li, Xueming
Kim, Ho Min
Singh, Chingakham Ranjit
Tian, Geng
Hoyt, Martin A.
Lovell, Scott
Battaile, Kevin P.
Zolkiewski, Michal
Coffino, Philip
Roelofs, Jeroen
Cheng, Yifan
Finley, Daniel
Reconfiguration of the proteasome during chaperone-mediated assembly
title Reconfiguration of the proteasome during chaperone-mediated assembly
title_full Reconfiguration of the proteasome during chaperone-mediated assembly
title_fullStr Reconfiguration of the proteasome during chaperone-mediated assembly
title_full_unstemmed Reconfiguration of the proteasome during chaperone-mediated assembly
title_short Reconfiguration of the proteasome during chaperone-mediated assembly
title_sort reconfiguration of the proteasome during chaperone-mediated assembly
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3687086/
https://www.ncbi.nlm.nih.gov/pubmed/23644457
http://dx.doi.org/10.1038/nature12123
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