2014年5月6日
Structural basis for proteasome formation controlled by an assembly chaperone nas2.
Structure (London, England : 1993)
- 巻
- 22
- 号
- 5
- 開始ページ
- 731
- 終了ページ
- 43
- 記述言語
- 英語
- 掲載種別
- 研究論文(学術雑誌)
- DOI
- 10.1016/j.str.2014.02.014
- 出版者・発行元
- CELL PRESS
Proteasome formation does not occur due to spontaneous self-organization but results from a highly ordered process assisted by several assembly chaperones. The assembly of the proteasome ATPase subunits is assisted by four client-specific chaperones, of which three have been structurally resolved. Here, we provide the structural basis for the working mechanisms of the last, hereto structurally uncharacterized assembly chaperone, Nas2. We revealed that Nas2 binds to the Rpt5 subunit in a bivalent mode: the N-terminal helical domain of Nas2 masks the Rpt1-interacting surface of Rpt5, whereas its C-terminal PDZ domain caps the C-terminal proteasome-activating motif. Thus, Nas2 operates as a proteasome activation blocker, offering a checkpoint during the formation of the 19S ATPase prior to its docking onto the proteolytic 20S core particle.
- リンク情報
-
- DOI
- https://doi.org/10.1016/j.str.2014.02.014
- PubMed
- https://www.ncbi.nlm.nih.gov/pubmed/24685148
- Web of Science
- https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000335443700011&DestApp=WOS_CPL
- Scopus
- https://www.scopus.com/inward/record.uri?partnerID=HzOxMe3b&scp=84899918113&origin=inward 本文へのリンクあり
- Scopus Citedby
- https://www.scopus.com/inward/citedby.uri?partnerID=HzOxMe3b&scp=84899918113&origin=inward
- ID情報
-
- DOI : 10.1016/j.str.2014.02.014
- ISSN : 0969-2126
- eISSN : 1878-4186
- PubMed ID : 24685148
- SCOPUS ID : 84899918113
- Web of Science ID : WOS:000335443700011