期刊
STRUCTURE
卷 22, 期 5, 页码 731-743出版社
CELL PRESS
DOI: 10.1016/j.str.2014.02.014
关键词
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资金
- Academia Sinica and NSRRC
- Japan Collection of Microorganisms [JCM 8422]
- JSPS KAKENHI [25121730, 22687009, 24112008, 21000012, 25102008, 24657113]
- Nanotechnology Platform Project
- Ministry of Education, Culture, Sports, Science and Technology, Japan
- Okazaki ORION project
- RIKEN BRC
- National BioResource Project of the MEXT, Japan
- Grants-in-Aid for Scientific Research [21000012, 25102001, 22687009, 24657097, 24770102, 25102008, 24657113, 26000014] Funding Source: KAKEN
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.
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