title: Histone acetylation: influence on transcription, nucleosome mobility and positioning, and linker histone-dependent transcriptional repression.
abstract: We demonstrate using a dinucleosome template that acetylation of the core histones enhances transcription by RNA polymerase III. This effect is not dependent on an increased mobility of the core histone octamer with respect to DNA sequence. When linker histone is subsequently bound, we find both a reduction in nucleosome mobility and a repression of transcription. These effects of linker histone binding are independent of core histone acetylation, indicating that core histone acetylation does not prevent linker histone binding and the concomitant transcriptional repression. These studies are complemented by the use of a Xenopus egg extract competent both for chromatin assembly on replicating DNA and for RNA polymerase III transcription. Incorporation of acetylated histones and lack of linker histones together facilitate transcription by >10-fold in this system; however, they have little independent effect on transcription. Thus core histone acetylation significantly facilitates transcription, but this effect is inhibited by the assembly of linker histones into chromatin.
authors.affiliation: Laboratory of Molecular Embryology, National Institute of Child Health and Human Development, NIH, Bethesda, MD 20892-5431, USA.
authors.forename: K
authors.initials: K
authors.lastname: Ura
authors.forename: H
authors.initials: H
authors.lastname: Kurumizaka
authors.forename: S
authors.initials: S
authors.lastname: Dimitrov
authors.forename: G
authors.initials: G
authors.lastname: Almouzni
authors.forename: A P
authors.initials: AP
authors.lastname: Wolffe
mesh_terms: D000107:Acetylation; D000123:Acetyltransferases / Q000378:metabolism; D000818:Animals; D002457:Cell Extracts; D002843:Chromatin / Q000378:metabolism; D004261:DNA Replication / Q000502:physiology; D005786:Gene Expression Regulation / Q000502:physiology; D006367:HeLa Cells; D051548:Histone Acetyltransferases; D006657:Histones / Q000737:chemistry / Q000378:metabolism*; D006801:Humans; D009707:Nucleosomes / Q000378:metabolism*; D009865:Oocytes; D012320:RNA Polymerase III / Q000378:metabolism; D012341:RNA, Ribosomal, 5S / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins; D014158:Transcription, Genetic / Q000502:physiology*; D014982:Xenopus laevis
chemical_list: D002457:Cell Extracts; D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D012341:RNA, Ribosomal, 5S; D029701:Saccharomyces cerevisiae Proteins; D000123:Acetyltransferases; D051548:Histone Acetyltransferases; D012320:RNA Polymerase III