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Structural and functional characterisation of a cell cycle associated HDAC1/2 complex reveals the structural basis for complex assembly and nucleosome targeting.

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posted on 2015-05-07, 10:41 authored by Toshimasa Itoh, Louise Fairall, Frederick W. Muskett, Charles P. Milano, Peter J. Watson, N. Arnaudo, Almutasem Saleh, Christopher J. Millard, Mohammed El-Mezgueldi, F. Martino, John W. R. Schwabe
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.

History

Citation

Nucleic Acids Research (27 February 2015) 43 (4): 2033-2044.

Author affiliation

/Organisation/COLLEGE OF MEDICINE, BIOLOGICAL SCIENCES AND PSYCHOLOGY/School of Biological Sciences/Department of Biochemistry

Version

  • VoR (Version of Record)

Published in

Nucleic Acids Research (27 February 2015) 43 (4): 2033-2044.

Publisher

Oxford University Press (OUP)

issn

0305-1048

eissn

1362-4962

Acceptance date

2015-01-19

Copyright date

2015

Available date

2015-08-21

Publisher version

http://nar.oxfordjournals.org/content/43/4/2033

Language

en

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