Journal
ELIFE
Volume 5, Issue -, Pages -Publisher
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.13941
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Funding
- Wellcome Trust [WT100237, 055663/Z/98/Z]
- Biotechnology and Biological Sciences Research Council [BB/J009598/1, BB/K003461/1]
- Royal Society
- BBSRC [BB/J009598/1, BB/N002954/1, BB/M01228X/1, BB/K003461/1] Funding Source: UKRI
- Biotechnology and Biological Sciences Research Council [BB/N002954/1, BB/K003461/1, BB/J009598/1, BB/M01228X/1] Funding Source: researchfish
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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.
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