title: Targeted recruitment of Set1 histone methylase by elongating Pol II provides a localized mark and memory of recent transcriptional activity.
abstract: Set1, the yeast histone H3-lysine 4 (H3-K4) methylase, is recruited by the Pol II elongation machinery to a highly localized domain at the 5' portion of active mRNA coding regions. Set1 association depends upon the TFIIH-associated kinase that phosphorylates the Pol II C-terminal domain (CTD) and mediates the transition between initiation and elongation, and Set1 interacts with the form of Pol II whose CTD is phosphorylated at serine 5 but not serine 2. The Rtf1 and Paf1 components of the Pol II-associated Paf1 complex are also important for Set1 recruitment. Although the level of dimethylated H3-K4 is fairly uniform throughout the genome, the pattern of trimethylated H3-K4 strongly correlates with Set1 occupancy. Hypermethylated H3-K4 within the mRNA coding region persists for considerable time after transcriptional inactivation and Set1 dissociation from the chromatin, indicating that H3-K4 hypermethylation provides a molecular memory of recent transcriptional activity.
authors.affiliation: Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
authors.forename: Huck Hui
authors.initials: HH
authors.lastname: Ng
authors.forename: François
authors.initials: F
authors.lastname: Robert
authors.forename: Richard A
authors.initials: RA
authors.lastname: Young
authors.forename: Kevin
authors.initials: K
authors.lastname: Struhl
mesh_terms: D015153:Blotting, Western; D019175:DNA Methylation; D004257:DNA Polymerase II / Q000378:metabolism*; D004268:DNA-Binding Proteins / Q000737:chemistry* / Q000378:metabolism*; D016681:Genome, Fungal; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones / Q000378:metabolism; D008025:Ligases / Q000378:metabolism; D008745:Methylation; D008957:Models, Genetic; D009687:Nuclear Proteins / Q000378:metabolism; D016366:Open Reading Frames; D010766:Phosphorylation; D011233:Precipitin Tests; D017434:Protein Structure, Tertiary; D012333:RNA, Messenger / Q000378:metabolism; D012441:Saccharomyces cerevisiae / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism*; D012694:Serine / Q000378:metabolism; D035181:TATA-Box Binding Protein / Q000378:metabolism; D014157:Transcription Factors / Q000737:chemistry* / Q000378:metabolism*; D014158:Transcription, Genetic; D044763:Ubiquitin-Conjugating Enzymes
chemical_list: D004268:DNA-Binding Proteins; D006657:Histones; D009687:Nuclear Proteins; C097698:PAF1 protein, S cerevisiae; D012333:RNA, Messenger; C107273:RTF1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; D035181:TATA-Box Binding Protein; D014157:Transcription Factors; D012694:Serine; D011495:Histone-Lysine N-Methyltransferase; C411250:SET1 protein, S cerevisiae; D044763:Ubiquitin-Conjugating Enzymes; D004257:DNA Polymerase II; D008025:Ligases