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Title: Structural and functional characterisation of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting.
Authors: Itoh, Toshimasa
Fairall, Louise
Muskett, Frederick W.
Milano, Charles P.
Watson, Peter J.
Arnaudo, N.
Saleh, Almutasem
Millard, Christopher J.
El-Mezgueldi, Mohammed
Martino, F.
Schwabe, John W. R.
First Published: 4-Feb-2015
Publisher: Oxford University Press (OUP)
Citation: Nucleic Acids Research (27 February 2015) 43 (4): 2033-2044.
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 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 aminoterminal region forms a tight dimerisation domain with a novel structural fold that interacts with and mediates assembly of the HDAC1:MIDEAS complex. The carboxyterminal 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.
DOI Link: 10.1093/nar/gkv068
ISSN: 0305-1048
eISSN: 1362-4962
Version: Published version (Publisher PDF)
Status: Peer-reviewed
Type: Journal Article
Rights: Copyright The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research. This is an Open Access article distributed under the terms of the Creative Commons Attribution License (, which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.
Appears in Collections:Published Articles, Dept. of Biochemistry

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