An atomic model AAA-ATPase/20S core particle sub-complex of the 26S proteasome

被引：49

作者：

Foerster, Friedrich ^{[1
,2
,3
]}

Lasker, Keren ^{[2
,3
,4
]}

Beck, Florian ^{[1
]}

Nickell, Stephan ^{[1
]}

Sali, Andrej ^{[2
,3
]}

Baumeister, Wolfgang ^{[1
]}

机构：

[1] Max Planck Inst Biochem, Dept Biol Struct, D-82152 Martinsried, Germany

[2] Univ Calif San Francisco, Dept Pharmaceut Chem, Dept Bioengn & Therapeut Sci, San Francisco, CA 94143 USA

[3] Univ Calif San Francisco, Calif Inst Quantitat Biosci QB3, San Francisco, CA 94143 USA

[4] Tel Aviv Univ, Raymond & Beverly Sackler Fac Exact Sci, Blavatnik Sch Comp Sci, IL-69978 Tel Aviv, Israel

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2009年 / 388卷 / 02期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

Proteasome; Protein degradation; Modeling; Assembly; cryo-EM; AAA-ATPase; 20S PROTEASOME; REGULATORY PARTICLE; 2-HYBRID ANALYSIS; SACCHAROMYCES-CEREVISIAE; CRYSTAL-STRUCTURE; SUBSTRATE ENTRY; ATPASE SUBUNIT; S PROTEASOME; YEAST; DEGRADATION;

D O I：

10.1016/j.bbrc.2009.07.145

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：228 / 233

页数：6

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