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J. Biol. Chem., Vol. 282, Issue 29, 21024-21031, July 20, 2007

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Purification and Characterization of Cellular Proteins Associated with Histone H4 Tails^*

Jongkyu Choi, Bong Kim, Kyu Heo, Kyunghwan Kim, Hyunjung Kim, Yuxia Zhan¹, Jeffrey A. Ranish, and Woojin An²

From the Department of Biochemistry and Molecular Biology, University of Southern California (USC)/Norris Comprehensive Cancer Center, USC Keck School of Medicine, Los Angeles, California 90033 and the Institute for Systems Biology, Seattle, Washington 98103

The histone H4 N-terminal tail has long been regarded as a major regulator in chromatin structure and function. Although the underlying mechanism has not been unraveled, an emerging body of evidence supports that H4 tail and its post-translational modification function as a recruitment motif for key factors required for proper regulation of chromatin transcription. To investigate these aspects, we have generated HeLa cell lines that constitutively express ectopic H4 tail domain for biochemical purification of proteins associated with H4 tail. We found that expressed H4 tails stably associate with sets of transcription regulatory factors and histone methyltransferases distinct from those that associate with histone H3 tails. Importantly, point mutations of four major lysine substrates to block cellular acetylation of ectopic H4 tail significantly inhibited the association of histone methyltransferases and sets of transcription-activating factors, supporting a major role of acetylation on recruitmentbased action of H4 tail during transcription. Further, our transcription analysis revealed that the proteins associated with wild-type/acetylated H4 tail, but not with mutant/unacetylated H4 tail, can enhance p300-dependent chromatin transcription. Taken together, these findings demonstrate novel roles for H4 tail and its acetylation in mediating recruitment of multiple regulatory factors that can change chromatin states for transcription regulation.

Received for publication, May 11, 2007 , and in revised form, June 1, 2007.

^* This work was supported in part by the Margaret E. Early Medical Research Trust. 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 Present address: Childrens Hospital Los Angeles, 4650 Sunset Blvd., SRT-1014, Los Angeles, CA 90027.

² A V-foundation scholar. To whom correspondence should be addressed: 1501 San Pablo St., ZNI. Rm. 241, University of Southern California, Los Angeles, CA 90033. Tel.: 323-442-4398; Fax: 323-442-4433; E-mail: woojinan{at}usc.edu.

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