title: Structure and mechanisms of lysine methylation recognition by the chromodomain in gene transcription.
abstract: Histone methylation recognition is accomplished by a number of evolutionarily conserved protein domains, including those belonging to the methylated lysine-binding Royal family of structural folds. One well-known member of the Royal family, the chromodomain, is found in the HP1/chromobox and CHD subfamilies of proteins, in addition to a small number of other proteins that are involved in chromatin remodeling and gene transcriptional silencing. Here we discuss the structure and function of the chromodomain within these proteins as methylated histone lysine binders and how the functions of these chromodomains can be modulated by additional post-translational modifications or binding to nucleic acids.
authors.affiliation: Department of Structural and Chemical Biology, Mount Sinai School of Medicine, One Gustave L. Levy Place, Box 1677, New York, New York 10065, United States.
authors.forename: Kyoko L
authors.initials: KL
authors.lastname: Yap
authors.forename: Ming-Ming
authors.initials: MM
authors.lastname: Zhou
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D002843:Chromatin / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D042002:Chromatin Assembly and Disassembly; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D008745:Methylation; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D014158:Transcription, Genetic
chemical_list: D002843:Chromatin; D008239:Lysine