Please use this identifier to cite or link to this item: http://hdl.handle.net/2381/32363
Title: Insights into the recruitment of class IIa Histone Deacetylases (HDACs) to the SMRT/NCoR transcriptional repression complex
Authors: Hudson, Gregg M.
Watson, Peter J.
Fairall, Louise
Jamieson, Andrew G.
Schwabe, John W. R.
First Published: 8-Jun-2015
Publisher: American Society for Biochemistry and Molecular Biology
Citation: Journal of Biological Chemistry, 2015 290, 18237-18244.
Abstract: Class IIa histone deacetylases repress transcription of target genes. However their mechanism of action is poorly understood since they exhibit very low levels of deacetylase activity. The class IIa HDACs are associated with the SMRT / NCoR re pression complexes and this may, at least in part, a ccount for their repressive activity. However, the molecular mechanism of recruitment to co - repressor proteins has yet to be established. Here we show that a repeated peptide motif present in both SMRT and NCoR is sufficient to mediate specific interaction , with micromolar affinity, with all the class IIa HDACs (HDACs 4, 5, 7 & 9). Mutations in the consensus motif abrogate binding. Mutational analysis of HDAC4 suggests that the peptide interacts in the vicinity of the active site of the enzyme and requires the “closed” conformation of the zinc - binding loop on the surface of the enzyme. Together these findings represent the first insights into the molecular mechanism of recruitment of class IIa HDACs to the SMRT / NCoR repression complexes.
DOI Link: 10.1074/jbc.M115.661058
ISSN: 0021-9258
1083-351X
Links: http://www.jbc.org/content/290/29/18237.short
http://hdl.handle.net/2381/32363
Version: Published version (Publisher PDF)
Status: Peer-reviewed
Type: Journal Article
Rights: © 2015 by The American Society for Biochemistry and Molecular Biology, Inc. Author's Choice—Final version free via Creative Commons CC-BY license http://creativecommons.org/licenses/by/3.0/.
Appears in Collections:Published Articles, Dept. of Biochemistry

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