Evidence map›Paper›PMID 27098840›Full record

ArticleeLife2016

The structure of the core NuRD repression complex provides insights into its interaction with chromatin.

Christopher J Millard, Niranjan Varma, Almutasem Saleh, Kyle Morris, Peter J Watson, Andrew R Bottrill, Louise Fairall, Corinne J Smith, John W R Schwabe

Open access · goldAbstract read
In one paragraph

Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
6.1field-weighted citation impact, top 3% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

92 citing papers in PubMed, 136 citations in OpenAlex.

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32 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 1 country.

Christopher J MillardHenry Wellcome Laboratories of Structural Biology, Department of Molecular and Cell Biology, University of Leicester, Leicester, United Kingdom.ORCID http://orcid.org/0000-0002-1012-0829
Niranjan VarmaHenry Wellcome Laboratories of Structural Biology, Department of Molecular and Cell Biology, University of Leicester, Leicester, United Kingdom.
Almutasem SalehHenry Wellcome Laboratories of Structural Biology, Department of Molecular and Cell Biology, University of Leicester, Leicester, United Kingdom.ORCID http://orcid.org/0000-0002-0156-4508
Kyle MorrisSchool of Life Sciences, University of Warwick, Coventry, United Kingdom.
Peter J WatsonHenry Wellcome Laboratories of Structural Biology, Department of Molecular and Cell Biology, University of Leicester, Leicester, United Kingdom.
Andrew R BottrillProtein and Nucleic Acid Chemistry Laboratory, Core Biotechnology Services, University of Leicester, Leicester, United Kingdom.ORCID http://orcid.org/0000-0002-5182-3643
Louise FairallHenry Wellcome Laboratories of Structural Biology, Department of Molecular and Cell Biology, University of Leicester, Leicester, United Kingdom.
Corinne J SmithSchool of Life Sciences, University of Warwick, Coventry, United Kingdom.
John W R SchwabeHenry Wellcome Laboratories of Structural Biology, Department of Molecular and Cell Biology, University of Leicester, Leicester, United Kingdom.ORCID http://orcid.org/0000-0003-2865-4383
University of Leicester · GBUniversity of Warwick · GB

Funding

Biotechnology and Biological Sciences Research Council BB/J009598/1Biotechnology and Biological Sciences Research Council BB/K003461/1Wellcome Trust 055663/Z/98/ZWellcome Trust 100237/Z/12/ZWellcome Trust WT100237
6 · The paper itself

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.

Indexed as

ChromatinCrystallography, X-RayHistone Deacetylase 1Histone Deacetylase 2Histone DeacetylasesMi-2 Nucleosome Remodeling and Deacetylase ComplexProtein ConformationRepressor ProteinsRetinoblastoma-Binding Protein 4Trans-ActivatorsChromatinHDAC1 protein, humanHDAC2 protein, humanHistone Deacetylase 1Histone Deacetylase 2Histone DeacetylasesMi-2 Nucleosome Remodeling and Deacetylase ComplexMTA1 protein, humanRBBP4 protein, humanRepressor ProteinsRetinoblastoma-Binding Protein 4Trans-Activatorsbiochemistrybiophysicschromatinhistone deacetylasehumanrepression complexstructural biologytranscription regulation

Identifiers

PMID27098840
PMCPMC4841774
OpenAlexW2340883705

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.