Journal
JOURNAL OF BIOLOGICAL CHEMISTRY
Volume 280, Issue 51, Pages 41789-41792Publisher
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.C500395200
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Funding
- NIGMS NIH HHS [R37 GM037120, GM-51966, F32 GM071166-02, R01 GM037120, F32 GM071166, GM-71166, GM-37120, F32 GM071166-01, R37 GM051966, R01 GM051966] Funding Source: Medline
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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 similar to 5 mu M, 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.
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