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CryoEM structures of the human INO80 chromatin remodelling complex

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Title: CryoEM structures of the human INO80 chromatin remodelling complex
Authors: Zhang, X
Aramayo, RJ
Willhoft, O
Ayala, R
Bythell-Douglas, R
Wigley, DB
Item Type: Journal Article
Abstract: Access to chromatin for processes such as DNA repair and transcription requires the sliding of nucleosomes along DNA. The multi-subunit INO80 chromatin remodelling complex has a particular role in DNA repair. Here we present the cryo electron microscopy structures of the active core complex of human INO80 at 9.6 Å with portions at 4.1 Å resolution along with 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 Tip49a (RUVBL1) and Tip49b (RUVBL2) AAA+ heterohexamer. An unusual spoked-wheel structural domain of the Ino80 subunit is engulfed by this heterohexamer and the intimate association of this Ino80 domain with the heterohexamer is at the core of the complex. We also identify a cleft in RUVBL1 and RUVBL2, which forms a major interaction site for partner proteins and likely communicates partner-interactions with its nucleotide binding sites.
Issue Date: 4-Dec-2017
Date of Acceptance: 1-Nov-2017
URI: http://hdl.handle.net/10044/1/54418
DOI: https://dx.doi.org/10.1038/s41594-017-0003-7
ISSN: 1545-9985
Publisher: Nature Publishing Group
Start Page: 37
End Page: 44
Journal / Book Title: Nature Structural and Molecular Biology
Volume: 25
Copyright Statement: Copyright © 2017, Springer Nature
Sponsor/Funder: Wellcome Trust
Institute of Cancer Research
The Royal Society
Imperial College Trust
Wellcome Trust
Wellcome Trust
Wellcome Trust
Cancer Research UK
Funder's Grant Number: 091093/B/09/Z
WEL078X-DBDBWJ-7947
WM110083
P43904
098412/Z/12/Z
WT/099128/Z/12/Z
095519/B/11/Z
12799
Keywords: 11 Medical And Health Sciences
03 Chemical Sciences
06 Biological Sciences
Biophysics
Developmental Biology
Publication Status: Published
Appears in Collections:Department of Medicine
Faculty of Medicine



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