Molecular Architecture of the ATP-Dependent Chromatin-Remodeling Complex SWR1

被引：127

作者：

Nguyen, Vu Q. ^{[1
]}

Ranjan, Anand ^{[2
]}

Stengel, Florian ^{[3
]}

Wei, Debbie ^{[2
]}

Aebersold, Ruedi ^{[3
,4
]}

Wu, Carl ^{[2
,5
]}

Leschziner, Andres E. ^{[1
]}

机构：

[1] Harvard Univ, Dept Mol & Cellular Biol, Cambridge, MA 02138 USA

[2] NCI, Lab Biochem & Mol Biol, Ctr Canc Res, Bethesda, MD 20892 USA

[3] ETH, Inst Mol Syst Biol, Dept Biol, CH-8092 Zurich, Switzerland

[4] Univ Zurich, Fac Sci, CH-8057 Zurich, Switzerland

[5] HHMI Janelia Farm Res Campus, Ashburn, VA 20147 USA

来源：

CELL | 2013年 / 154卷 / 06期

基金：

美国国家科学基金会; 美国国家卫生研究院;

关键词：

NUCLEOSOME CORE PARTICLE; ACTIN-RELATED PROTEINS; ELECTRON-MICROSCOPY; CRYSTAL-STRUCTURE; CONFORMATIONAL-CHANGES; HISTONE H2AZ; DOMAIN; REVEALS; TILT; RSC;

D O I：

10.1016/j.cell.2013.08.018

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 ATP-dependent chromatin-remodeling complex SWR1 exchanges a variant histone H2A.Z/H2B dimer for a canonical H2A/H2B dimer at nucleosomes flanking histone-depleted regions, such as promoters. This localization of H2A.Z is conserved throughout eukaryotes. SWR1 is a 1 megadalton complex containing 14 different polypeptides, including the AAA+ ATPases Rvb1 and Rvb2. Using electron microscopy, we obtained the three-dimensional structure of SWR1 and mapped its major functional components. Our data show that SWR1 contains a single heterohexameric Rvb1/Rvb2 ring that, together with the catalytic subunit Swr1, brackets two independently assembled multisubunit modules. We also show that SWR1 undergoes a large conformational change upon engaging a limited region of the nucleosome core particle. Our work suggests an important structural role for the Rvbs and a distinct substrate-handling mode by SWR1, thereby providing a structural framework for understanding the complex dimer-exchange reaction.

引用

页码：1220 / 1231

页数：12

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