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A more recent version of this article appeared on December 23, 2005
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C500395200v1
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Papers In Press, published online ahead of print October 31, 2005
J. Biol. Chem, 10.1074/jbc.C500395200
Submitted on September 26, 2005
Revised on October 27, 2005
Accepted on October 31, 2005

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

Biochemistry Dept., HHMI-RWJMS, Piscataway, NJ 08854

Corresponding Author: reinbedf{at}umdnj.edu

Defining the protein factors that directly recognize post-translational, covalent histone modifications is essential towards 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 tri-methyl H3K4 with a dissociation constant of approximately 5 µM, whereas mono-methyl H3K4 binds CHD1 with a three-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.


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