title: Histone methyltransferases direct different degrees of methylation to define distinct chromatin domains.
abstract: The functional significance of mono-, di-, and trimethylation of lysine residues within histone proteins remains unclear. Antibodies developed to selectively recognize each of these methylated states at histone H3 lysine 9 (H3 Lys9) demonstrated that mono- and dimethylation localized specifically to silent domains within euchromatin. In contrast, trimethylated H3 Lys9 was enriched at pericentric heterochromatin. Enzymes known to methylate H3 Lys9 displayed remarkably different enzymatic properties in vivo. G9a was responsible for all detectable H3 Lys9 dimethylation and a significant amount of monomethylation within silent euchromatin. In contrast, Suv39h1 and Suv39h2 directed H3 Lys9 trimethylation specifically at pericentric heterochromatin. Thus, different methylated states of H3 Lys9 are directed by specific histone methyltransferases to "mark" distinct domains of silent chromatin.
authors.affiliation: Department of Biochemistry and Molecular Genetics, University of Virginia Health System, University of Virginia, Charlottesville, VA 22908, USA.
authors.forename: Judd C
authors.initials: JC
authors.lastname: Rice
authors.forename: Scott D
authors.initials: SD
authors.lastname: Briggs
authors.forename: Beatrix
authors.initials: B
authors.lastname: Ueberheide
authors.forename: Cynthia M
authors.initials: CM
authors.lastname: Barber
authors.forename: Jeffrey
authors.initials: J
authors.lastname: Shabanowitz
authors.forename: Donald F
authors.initials: DF
authors.lastname: Hunt
authors.forename: Yoichi
authors.initials: Y
authors.lastname: Shinkai
authors.forename: C David
authors.initials: CD
authors.lastname: Allis
mesh_terms: D000818:Animals; D002478:Cells, Cultured; D002843:Chromatin / Q000378:metabolism*; D005347:Fibroblasts / Q000166:cytology / Q000378:metabolism; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000378:metabolism*; D008745:Methylation; D008780:Methyltransferases / Q000378:metabolism; D051379:Mice; D011496:Protein Methyltransferases; D012097:Repressor Proteins / Q000378:metabolism; D014158:Transcription, Genetic
chemical_list: D002843:Chromatin; D006657:Histones; D012097:Repressor Proteins; C407843:SUV39H1 protein, human; C498700:Suv39h1 protein, mouse; D000076983:Histone Methyltransferases; D008780:Methyltransferases; D011496:Protein Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D008239:Lysine