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Title | Structural and functional characterization of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting. |
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Journal, issue, pages | Nucleic Acids Res, Vol. 43, Issue 4, Page 2033-2044, Year 2015 |
Publish date | Feb 27, 2015 |
Authors | Toshimasa Itoh / Louise Fairall / Frederick W Muskett / Charles P Milano / Peter J Watson / Nadia Arnaudo / Almutasem Saleh / Christopher J Millard / Mohammed El-Mezgueldi / Fabrizio Martino / John W R Schwabe / |
PubMed Abstract | 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 ...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. |
External links | Nucleic Acids Res / PubMed:25653165 / PubMed Central |
Methods | NMR (solution) / X-ray diffraction |
Resolution | 2.1 Å |
Structure data | PDB-2mwi: PDB-4d6k: |
Chemicals | ChemComp-HOH: |
Source |
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Keywords | PROTEIN BINDING / HDAC / histone deacetylase / gene expression / DNTTIP1 / MIDEAS / HDAC1 / TDIF1 / TRANSCRIPTION / HISTONE DEACETYLASE COMPLEX |