title: Differential chromatin marking of introns and expressed exons by H3K36me3.
abstract: Variation in patterns of methylations of histone tails reflects and modulates chromatin structure and function. To provide a framework for the analysis of chromatin function in Caenorhabditis elegans, we generated a genome-wide map of histone H3 tail methylations. We find that C. elegans genes show distributions of histone modifications that are similar to those of other organisms, with H3K4me3 near transcription start sites, H3K36me3 in the body of genes and H3K9me3 enriched on silent genes. We also observe a novel pattern: exons are preferentially marked with H3K36me3 relative to introns. H3K36me3 exon marking is dependent on transcription and is found at lower levels in alternatively spliced exons, supporting a splicing-related marking mechanism. We further show that the difference in H3K36me3 marking between exons and introns is evolutionarily conserved in human and mouse. We propose that H3K36me3 exon marking in chromatin provides a dynamic link between transcription and splicing.
authors.affiliation: The Gurdon Institute and Department of Genetics, University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK.
authors.forename: Paulina
authors.initials: P
authors.lastname: Kolasinska-Zwierz
authors.forename: Thomas
authors.initials: T
authors.lastname: Down
authors.forename: Isabel
authors.initials: I
authors.lastname: Latorre
authors.forename: Tao
authors.initials: T
authors.lastname: Liu
authors.forename: X Shirley
authors.initials: XS
authors.lastname: Liu
authors.forename: Julie
authors.initials: J
authors.lastname: Ahringer
mesh_terms: D017398:Alternative Splicing / Q000235:genetics; D000818:Animals; D001665:Binding Sites; D017173:Caenorhabditis elegans / Q000235:genetics / Q000378:metabolism; D002843:Chromatin / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D002874:Chromosome Mapping; D005091:Exons; D005786:Gene Expression Regulation / Q000502:physiology; D020868:Gene Silencing / Q000502:physiology; D000076983:Histone Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D006657:Histones / Q000378:metabolism*; D007438:Introns; D008239:Lysine / Q000378:metabolism*; D008745:Methylation; D016366:Open Reading Frames / Q000502:physiology; D011485:Protein Binding / Q000502:physiology; D011496:Protein Methyltransferases / Q000378:metabolism*; D014158:Transcription, Genetic / Q000502:physiology
chemical_list: D002843:Chromatin; D006657:Histones; D000076983:Histone Methyltransferases; D011496:Protein Methyltransferases; D011495:Histone-Lysine N-Methyltransferase; D008239:Lysine