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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...
Autores principales: | , , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2013
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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. |
format | Online Article Text |
id | pubmed-3687086 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
record_format | MEDLINE/PubMed |
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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