title: The Paf1 complex is required for histone H3 methylation by COMPASS and Dot1p: linking transcriptional elongation to histone methylation.
abstract: Methylation of histone proteins is one of their many modifications that affect chromatin structure and regulate gene expression. Methylation of histone H3 on lysines 4 and 79, catalyzed by the Set1-containing complex COMPASS and Dot1p, respectively, is required for silencing of expression of genes located near chromosome telomeres in yeast. We report that the Paf1 protein complex, which is associated with the elongating RNA polymerase II, is required for methylation of lysines 4 and 79 of histone H3 and for silencing of expression of a telomere-associated gene. We show that the Paf1 complex is required for recruitment of the COMPASS methyltransferase to RNA polymerase II and that the subunits of these complexes interact physically and genetically. Collectively, our results suggest that the Paf1 complex is required for histone H3 methylation, therefore linking transcriptional elongation to chromatin methylation.
authors.affiliation: Banting and Best Department of Medical Research, Department of Molecular and Medical Genetics, University of Toronto, Toronto, M5G 1L6, Ontario, Canada.
authors.forename: Nevan J
authors.initials: NJ
authors.lastname: Krogan
authors.forename: Jim
authors.initials: J
authors.lastname: Dover
authors.forename: Adam
authors.initials: A
authors.lastname: Wood
authors.forename: Jessica
authors.initials: J
authors.lastname: Schneider
authors.forename: Jonathan
authors.initials: J
authors.lastname: Heidt
authors.forename: Marry Ann
authors.initials: MA
authors.lastname: Boateng
authors.forename: Kimberly
authors.initials: K
authors.lastname: Dean
authors.forename: Owen W
authors.initials: OW
authors.lastname: Ryan
authors.forename: Ashkan
authors.initials: A
authors.lastname: Golshani
authors.forename: Mark
authors.initials: M
authors.lastname: Johnston
authors.forename: Jack F
authors.initials: JF
authors.lastname: Greenblatt
authors.forename: Ali
authors.initials: A
authors.lastname: Shilatifard
mesh_terms: D015153:Blotting, Western; D002843:Chromatin / Q000378:metabolism; D019175:DNA Methylation; D004268:DNA-Binding Proteins / Q000378:metabolism*; D004591:Electrophoresis, Polyacrylamide Gel; D020868:Gene Silencing; D016681:Genome, Fungal; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones / Q000378:metabolism*; D008239:Lysine / Q000737:chemistry; D008745:Methylation; D008780:Methyltransferases / Q000737:chemistry / Q000378:metabolism*; D008957:Models, Genetic; D009154:Mutation; D009687:Nuclear Proteins / Q000378:metabolism*; D011233:Precipitin Tests; D011485:Protein Binding; D011496:Protein Methyltransferases; D020543:Proteome; D012319:RNA Polymerase II / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000235:genetics* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*; D016615:Telomere / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism*; D014158:Transcription, Genetic
chemical_list: D002843:Chromatin; D004268:DNA-Binding Proteins; D006657:Histones; D009687:Nuclear Proteins; C097698:PAF1 protein, S cerevisiae; D020543:Proteome; D029701:Saccharomyces cerevisiae Proteins; D014157:Transcription Factors; D000076983:Histone Methyltransferases; D008780:Methyltransferases; D011496:Protein Methyltransferases; C416235:Dot1 protein, S cerevisiae; D011495:Histone-Lysine N-Methyltransferase; C411250:SET1 protein, S cerevisiae; D012319:RNA Polymerase II; D008239:Lysine