Insights into the molecular architecture of the 26S proteasome

被引：100

作者：

Nickell, Stephan

Beck, Florian

Scheres, Sjors H. W. ^{[2
]}

Korinek, Andreas

Foerster, Friedrich ^{[3
]}

Lasker, Keren ^{[3
,4
]}

Mihalache, Oana

Sun, Na

Nagya, Istvan

Sali, Andrej ^{[3
]}

Plitzko, Juergen M.

Carazo, Jose-Maria ^{[2
]}

Mann, Matthias

Baumeister, Wolfgang ^{[1
]}

机构：

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

[2] Ctr Nacl Biotecnol, Consejo Super Invest Cient, Madrid 28049, Spain

[3] Univ Calif San Francisco, Dept Bioengn & Therapeut Sci, San Francisco, CA 94158 USA

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

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2009年 / 106卷 / 29期

基金：

美国国家卫生研究院; 美国国家科学基金会;

关键词：

ATPase; cryo-electron microscopy; mass spectrometry; protein degradation; AAA-ATPase; 20S PROTEASOME; ELECTRON-MICROSCOPY; REGULATORY PARTICLE; CRYOELECTRON MICROSCOPY; ANGSTROM RESOLUTION; COMPLEX; RECONSTRUCTION; PROTEINS; MACROMOLECULES; DEGRADATION;

D O I：

10.1073/pnas.0905081106

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Cryo-electron microscopy in conjunction with advanced image analysis was used to analyze the structure of the 26S proteasome and to elucidate its variable features. We have been able to outline the boundaries of the ATPase module in the "base'' part of the regulatory complex that can vary in its position and orientation relative to the 20S core particle. This variation is consistent with the "wobbling'' model that was previously proposed to explain the role of the regulatory complex in opening the gate in the alpha-rings of the core particle. In addition, a variable mass near the mouth of the ATPase ring has been identified as Rpn10, a multiubiquitin receptor, by correlating the electron microscopy data with quantitative mass spectrometry.

引用

页码：11943 / 11947

页数：5

共 41 条

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