期刊
NUCLEIC ACIDS RESEARCH
卷 43, 期 4, 页码 2033-2044出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gkv068
关键词
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资金
- Wellcome Trust Programme
- [WT085408]
- [WT100237]
- Medical Research Council [MC_U105184333, MC_PC_14117] Funding Source: researchfish
- MRC [MC_PC_14117, MC_U105184333] Funding Source: UKRI
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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