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J. Biol. Chem., Vol. 282, Issue 45, 33227-33236, November 9, 2007

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Differential Distribution of Unmodified and Phosphorylated Histone Deacetylase 2 in Chromatin^*

From the Manitoba Institute of Cell Biology, University of Manitoba, Winnipeg, Manitoba R3E 0V9, Canada

Histone deacetylase 2 (HDAC2) is one of the histone-modifying enzymes that regulate gene expression by remodeling chromatin structure. Along with HDAC1, HDAC2 is found in the Sin3 and NuRD multiprotein complexes, which are recruited to promoters by DNA-binding proteins. In this study, we show that the majority of HDAC2 in human breast cancer cells is not phosphorylated. However, the minor population of HDAC2, preferentially cross-linked to DNA by cisplatin, is mono-, di-, or tri-phosphorylated. Furthermore, HDAC2 phosphorylation is required for formation of Sin3 and NuRD complexes and recruitment to promoters by transcription factors including p53, Rb, YY1, NF-B, Sp1, and Sp3. Unmodified HDAC2 requires linker DNA to associate with chromatin but is not cross-linked to DNA by formaldehyde. We provide evidence that unmodified HDAC2 is associated with the coding region of transcribed genes, whereas phosphorylated HDAC2 is primarily recruited to promoters.

Received for publication, April 27, 2007 , and in revised form, September 6, 2007.

^* This work was supported by Canadian Institute of Health Research Grant MOP-9186 and a Canada Research Chair (to J. R. D.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Manitoba Institute of Cell Biology, 675 McDermot Ave., Winnipeg, Manitoba R3E 0V9, Canada. Tel.: 204-787-2391; Fax: 204-787-2190; E-mail: davie{at}cc.umanitoba.ca.

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