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Itoh, Toshimasa; Fairall, Louise; Muskett, Frederick W; Milano, Charles P; Watson, Peter J; Arnaudo, Nadia; Saleh, Almutasem; Millard, Christopher J; El-Mezgueldi, Mohammed; Martino, Fabrizio; Schwabe, John W R
Nucleic acids research, 02/2015, Volume: 43, Issue: 4Journal Article
Recent proteomic studies have identified a novel histone deacetylase complex that is upregulated during mitosis and is associated with cyclin A. This complex is conserved from nematodes to man and contains histone deacetylases 1 and 2, the MIDEAS corepressor protein and a protein called DNTTIP1 whose function was hitherto poorly understood. Here, we report the structures of two domains from DNTTIP1. The amino-terminal region forms a tight dimerization domain with a novel structural fold that interacts with and mediates assembly of the HDAC1:MIDEAS complex. The carboxy-terminal domain of DNTTIP1 has a structure related to the SKI/SNO/DAC domain, despite lacking obvious sequence homology. We show that this domain in DNTTIP1 mediates interaction with both DNA and nucleosomes. Thus, DNTTIP1 acts as a dimeric chromatin binding module in the HDAC1:MIDEAS corepressor complex.
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