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-Structure paper
Title | The structure of the core NuRD repression complex provides insights into its interaction with chromatin. |
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Journal, issue, pages | Elife, Vol. 5, Page e13941, Year 2016 |
Publish date | Apr 21, 2016 |
Authors | Christopher J Millard / Niranjan Varma / Almutasem Saleh / Kyle Morris / Peter J Watson / Andrew R Bottrill / Louise Fairall / Corinne J Smith / John W R Schwabe / |
PubMed 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 ...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. |
External links | Elife / PubMed:27098840 / PubMed Central |
Methods | EM (single particle) / X-ray diffraction |
Resolution | 2.8 - 19.0 Å |
Structure data | EMDB-3399: PDB-5fxy: PDB-6g16: |
Source |
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Keywords | TRANSCRIPTION / TRANSCRIPTION REPRESSION COMPLEX METASTASIS ASSOCIATED COMPLEX MTA1 RBBP4 RBBP7 HISTONE BINDING PROTEIN / WD40 / corepressor / metastasis |