TY - JOUR TI - The structure of the core NuRD repression complex provides insights into its interaction with chromatin AU - Millard, Christopher J AU - Varma, Niranjan AU - Saleh, Almutasem AU - Morris, Kyle AU - Watson, Peter J AU - Bottrill, Andrew R AU - Fairall, Louise AU - Smith, Corinne J AU - Schwabe, John WR A2 - Workman, Jerry L VL - 5 PY - 2016 DA - 2016/04/21 SP - e13941 C1 - eLife 2016;5:e13941 DO - 10.7554/eLife.13941 UR - https://doi.org/10.7554/eLife.13941 AB - 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. KW - transcription regulation KW - histone deacetylase KW - repression complex KW - chromatin JF - eLife SN - 2050-084X PB - eLife Sciences Publications, Ltd ER -