title: Implications of a histone code mimic in epigenetic signaling.
abstract: In this issue of Molecular Cell, Sampath et al. show a lysine methylase exhibits substrate promiscuity and variability in degree of product methylation (Sampath et al., 2007). Two lysines are found to be automethylated in G9a, and one is H3K9-like and can establish a docking site for HP1 chromodomain.
authors: Department of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, VA 22908-0733, USA.
authors: Christopher H
authors: CH
authors: Henkels
authors: Sepideh
authors: S
authors: Khorasanizadeh
mesh_terms: D000818:Animals; D044127:Epigenesis, Genetic; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase / Q000737:chemistry / Q000378:metabolism; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000378:metabolism; D008745:Methylation; D051379:Mice; D018716:Molecular Mimicry; D011496:Protein Methyltransferases; D015398:Signal Transduction; D013379:Substrate Specificity
chemical_list: D006657:Histones; D000076983:Histone Methyltransferases; D011496:Protein Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D008239:Lysine