Connecting the DOTs: covalent histone modifications and the formation of silent chromatin.
Histone methylation has emerged as a significant regulator of chromatin structure and function. Two different classes of histone methyltransferase (HMT) have been described, which target either lysine or arginine residues in the histone N-terminal tails. A flurry of recent papers now describe a third class of HMT that affects chromatin silencing indirectly, not by methylation of histone tails, but instead by targeting a conserved lysine residue in the core domain of the nucleosome.
Asad U
AU
Khan
Michael
M
Hampsey
D000818:Animals; D020868:Gene Silencing / Q000502:physiology*; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D008780:Methyltransferases / Q000502:physiology*; D009687:Nuclear Proteins / Q000502:physiology; D011496:Protein Methyltransferases; D029701:Saccharomyces cerevisiae Proteins
D006657:Histones; D009687:Nuclear Proteins; D029701:Saccharomyces cerevisiae Proteins; D000076983:Histone Methyltransferases; D008780:Methyltransferases; D011496:Protein Methyltransferases; C416235:Dot1 protein, S cerevisiae; D011495:Histone-Lysine N-Methyltransferase