期刊
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
卷 388, 期 2, 页码 228-233出版社
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2009.07.145
关键词
Proteasome; Protein degradation; Modeling; Assembly; cryo-EM; AAA-ATPase
资金
- Human Frontier Science Project Organization (HFSPO)
- Tel Aviv University
- Clore Foundation
- European Commission [3-D]
- DFG
- Sandler Family Supporting Foundation
- National Institutes of Health [R01 GM54762, U54 RR022220, PN2 EY016525, R01 GM083960]
- National Science Foundation [IIS-0705196]
- Ron Conway
- Mike Homer
- Hewlett-Packard
- NetApp
- IBM
- Intel
The 26S proteasome is the most downstream element of the ubiquitin-proteasome pathway of protein degradation. It is composed of the 20S core particle (CP) and the 19S regulatory particle (RP). The RP consists of 6 AAA-ATPases and at least 13 non-ATPase subunits. Based on a cryo-EM map of the 26S proteasome, structures of homologs, and physical protein-protein interactions we derive an atomic model of the AAA-ATPase-CP sub-complex. The ATPase order in our model (Rpt1/Rpt2/Rpt6/Rpt3/Rpt4/Rpt5) is in excellent agreement with the recently identified base-precursor complexes formed during the assembly of the RP. Furthermore, the atomic CP-AAA-ATPase model suggests that the assembly chaperone Nas6 facilitates CP-RP association by enhancing the shape complementarity between Rpt3 and its binding CP alpha subunits partners. (C) 2009 Elsevier Inc. All rights reserved.
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