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J. Biol. Chem., Vol. 280, Issue 51, 41789-41792, December 23, 2005

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Human but Not Yeast CHD1 Binds Directly and Selectively to Histone H3 Methylated at Lysine 4 via Its Tandem Chromodomains^*

Robert J. Sims, III, Chi-Fu Chen, Helena Santos-Rosa, Tony Kouzarides, Smita S. Patel, and Danny Reinberg¶1

From the ^¶Howard Hughes Medical Institute and Division of Nucleic Acids Enzymology, Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, New Jersey 08854 and The Wellcome Trust/Cancer Research UK Gurdon Institute, Department of Pathology, University of Cambridge, Tennis Court Road, Cambridge CB2 1QR, United Kingdom

Defining the protein factors that directly recognize post-translational, covalent histone modifications is essential toward understanding the impact of these chromatin "marks" on gene regulation. In the current study, we identify human CHD1, an ATP-dependent chromatin remodeling protein, as a factor that directly and selectively recognizes histone H3 methylated on lysine 4. In vitro binding studies identified that CHD1 recognizes di- and trimethyl H3K4 with a dissociation constant (K_d) of 5 µM, whereas monomethyl H3K4 binds CHD1 with a 3-fold lower affinity. Surprisingly, human CHD1 binds to methylated H3K4 in a manner that requires both of its tandem chromodomains. In vitro analyses demonstrate that unlike human CHD1, yeast Chd1 does not bind methylated H3K4. Our findings indicate that yeast and human CHD1 have diverged in their ability to discriminate covalently modified histones and link histone modification-recognition and non-covalent chromatin remodeling activities within a single human protein.

Received for publication, September 26, 2005 , and in revised form, October 27, 2005.

^* This work was supported by the Howard Hughes Medical Institute (to D. R.) and National Institutes of Health Grants GM-37120 (to D. R.), GM-71166 (to R. J. S.), and GM-51966 (to S. S. P.). 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: Howard Hughes Medical Inst. and Division of Nucleic Acids Enzymology, Dept. of Biochemistry, Robert Wood Johnson Medical School, 683 Hoes Lane, Piscataway, NJ 08854. Tel.: 732-235-4195; Fax: 732-235-5294; E-mail: reinbedf{at}umdnj.edu.

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