Cryo-EM structures of the human INO80 chromatin-remodeling complex

被引：53

作者：

Aramayo, Ricardo J. ^{[1
]}

Willhoft, Oliver ^{[1
]}

Ayala, Rafael ^{[1
]}

Bythell-Douglas, Rohan ^{[1
]}

Wigley, Dale B. ^{[1
]}

Zhang, Xiaodong ^{[1
]}

机构：

[1] Imperial Coll London, Dept Med, Sect Struct Biol, London, England

来源：

NATURE STRUCTURAL & MOLECULAR BIOLOGY | 2018年 / 25卷 / 01期

基金：

英国惠康基金;

关键词：

ACTIN-RELATED PROTEINS; CRYSTAL-STRUCTURE; ATPASE; BINDING; DOMAIN; TRANSCRIPTION; ARCHITECTURE; MECHANISMS; RESOLUTION; ALIGNMENT;

D O I：

10.1038/s41594-017-0003-7

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：

Access to chromatin for processes such as transcription and DNA repair requires the sliding of nucleosomes along DNA. This process is aided by chromatin-remodeling complexes, such as the multisubunit INO80 chromatin-remodeling complex. Here we present cryo-EM structures of the active core complex of human INO80 at 9.6 angstrom, with portions at 4.1-angstrom resolution, and reconstructions of combinations of subunits. Together, these structures reveal the architecture of the INO80 complex, including Ino80 and actin-related proteins, which is assembled around a single RUVBL1 (Tip49a) and RUVBL2 (Tip49b) AAA+ heterohexamer. An unusual spoked-wheel structural domain of the Ino80 subunit is engulfed by this heterohexamer; both, in combination, form the core of the complex. We also identify a cleft in RUVBL1 and RUVBL2, which forms a major interaction site for partner proteins and probably communicates these interactions to its nucleotide-binding sites.

引用

页码：37 / +

页数：10

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