Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/37358
Title: The structure of the core NuRD complex provides insights into its interaction with chromatin
Authors: Millard, Christopher J.
Varma, Niranjan
Saleh, Almutasem
Morris, Kyle Morris
Watson, Peter J.
Bottrill, Andrew R
Fairall, Louise Fairall
Smith, Corinne J.
Schwabe, John W. R.
First Published: 2016
Publisher: eLife Sciences Publications
Citation: eLife, 2016, in press.
Abstract: The NuRD complex is a multi-protein transcriptional corepressor that couples histone deacetylase and ATP-dependent chromatin remodelling activities. The complex regulates the higher-order structure of chromatin, and has important roles in the regulation of gene expression, DNA damage repair and cell differentiation. HDACs 1 and 2 are recruited by the MTA1 corepressor to form the catalytic core of the complex. The histone chaperone protein RBBP4, has previously been shown to bind to the carboxy-terminal tail of MTA1. We show that MTA1 recruits a second copy of RBBP4. The crystal structure reveals an extensive interface between MTA1 and RBBP4. An EM structure, supported by SAXS and crosslinking, reveals the architecture of the dimeric HDAC1:MTA1:RBBP4 assembly which forms the core of the NuRD complex. We find evidence that in this complex RBBP4 mediates interaction with histone H3 tails, but not histone H4, suggesting a mechanism for recruitment of the NuRD complex to chromatin.
DOI Link: tba
eISSN: 2050-084X
Links: http://elifesciences.org/
http://hdl.handle.net/2381/37358
Embargo on file until: 1-Jan-10000
Version: Post-print
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright © the authors, 2016. This is an open-access article distributed under the terms of the Creative Commons Attribution License ( http://creativecommons.org/licenses/by/3.0/ ), which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
Description: Following publication the file associated with this record will be available under the license above.
Appears in Collections:Published Articles, Dept. of Molecular and Cell Biology

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