Structure of the 26S proteasome from Schizosaccharomyces pombe at subnanometer resolution

被引：110

作者：

Bohn, Stefan ^{[1
]}

Beck, Florian ^{[1
]}

Sakata, Eri ^{[1
]}

Walzthoeni, Thomas ^{[2
]}

Beck, Martin ^{[2
]}

Aebersold, Ruedi ^{[2
,3
]}

Foerster, Friedrich ^{[1
]}

Baumeister, Wolfgang ^{[1
]}

Nickell, Stephan ^{[1
]}

机构：

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

[2] ETH, Inst Mol Syst Biol, CH-8093 Zurich, Switzerland

[3] Univ Zurich, Fac Sci, CH-8093 Zurich, Switzerland

来源：

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA | 2010年 / 107卷 / 49期

基金：

日本学术振兴会;

关键词：

deubiquitylating enzymes; macromolecular complex; ubiquitin-proteasome pathway; ubiquitin receptor; single particle classification; MASS-SPECTROMETRY; CROSS-LINKING; METHANOCALDOCOCCUS-JANNASCHII; REGULATORY PARTICLE; UBIQUITIN SYSTEM; 20S PROTEASOME; PROTEIN; COMPLEXES; INSIGHTS; DEUBIQUITINATION;

D O I：

10.1073/pnas.1015530107

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：

The structure of the 26S proteasome from Schizosaccharomyces pombe has been determined to a resolution of 9.1 angstrom by cryoelectron microscopy and single particle analysis. In addition, chemical cross-linking in conjunction with mass spectrometry has been used to identify numerous residue pairs in close proximity to each other, providing an array of spatial restraints. Taken together these data clarify the topology of the AAA-ATPase module in the 19S regulatory particle and its spatial relationship to the a-ring of the 20S core particle. Image classification and variance analysis reveal a belt of high "activity" surrounding the AAA-ATPase module which is tentatively assigned to the reversible association of proteasome interacting proteins and the conformational heterogeneity among the particles. An integrated model is presented which sheds light on the early steps of protein degradation by the 26S complex.

引用

页码：20992 / 20997

页数：6

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