title: Histone H3 lysine 36 dimethylation (H3K36me2) is sufficient to recruit the Rpd3s histone deacetylase complex and to repress spurious transcription.
abstract: Histone methylation is associated with both transcription activation and repression. However, the functions of different states of methylation remain largely elusive. Here, using methyl-lysine analog technology, we demonstrate that the histone deacetylase complex, Rpd3S, can distinguish the nucleosomes methylated to different extents and that K36me2 is sufficient to target Rpd3S in vitro. Through a genome-wide survey, we identified a few mutants in which the level of K36me3 is significantly reduced, whereas the level of K36me2 is sustained. Transcription analysis and genome-wide histone modification studies on these mutants suggested that K36me2 is sufficient to target Rpd3S in vivo, thereby maintaining a functional Set2-Rpd3S pathway.
authors.affiliation: Stowers Institute for Medical Research, Kansas City, Missouri 64110, USA.
authors.forename: Bing
authors.initials: B
authors.lastname: Li
authors.forename: Jessica
authors.initials: J
authors.lastname: Jackson
authors.forename: Matthew D
authors.initials: MD
authors.lastname: Simon
authors.forename: Brian
authors.initials: B
authors.lastname: Fleharty
authors.forename: Madelaine
authors.initials: M
authors.lastname: Gogol
authors.forename: Chris
authors.initials: C
authors.lastname: Seidel
authors.forename: Jerry L
authors.initials: JL
authors.lastname: Workman
authors.forename: Ali
authors.initials: A
authors.lastname: Shilatifard
mesh_terms: D000818:Animals; D015894:Genome, Human / Q000502:physiology; D006367:HeLa Cells; D056464:Histone Deacetylase 2; D006655:Histone Deacetylases / Q000235:genetics / Q000378:metabolism*; D011495:Histone-Lysine N-Methyltransferase / Q000235:genetics / Q000378:metabolism; D006657:Histones / Q000235:genetics / Q000378:metabolism*; D006801:Humans; D008239:Lysine / Q000235:genetics / Q000378:metabolism*; D008745:Methylation; D009097:Multienzyme Complexes / Q000235:genetics / Q000378:metabolism*; D009154:Mutation; D012097:Repressor Proteins / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic / Q000502:physiology*; D014981:Xenopus
chemical_list: D006657:Histones; D009097:Multienzyme Complexes; D012097:Repressor Proteins; D011495:Histone-Lysine N-Methyltransferase; C521636:SETD2 protein, human; D056464:Histone Deacetylase 2; D006655:Histone Deacetylases; D008239:Lysine