title: Genome-wide H4 K16 acetylation by SAS-I is deposited independently of transcription and histone exchange.
abstract: The MYST HAT Sas2 is part of the SAS-I complex that acetylates histone H4 lysine 16 (H4 K16Ac) and blocks the propagation of heterochromatin at the telomeres of Saccharomyces cerevisiae. In this study, we investigated Sas2-mediated H4 K16Ac on a genome-wide scale. Interestingly, H4 K16Ac loss in sas2Δ cells outside of the telomeric regions showed a distinctive pattern in that there was a pronounced decrease of H4 K16Ac within the majority of open reading frames (ORFs), but little change in intergenic regions. Furthermore, regions of low histone H3 exchange and low H3 K56 acetylation showed the most pronounced loss of H4 K16Ac in sas2Δ, indicating that Sas2 deposited this modification on chromatin independently of histone exchange. In agreement with the effect of Sas2 within ORFs, sas2Δ caused resistance to 6-azauracil, indicating a positive effect on transcription elongation in the absence of H4 K16Ac. In summary, our data suggest that Sas2-dependent H4 K16Ac is deposited into chromatin independently of transcription and histone exchange, and that it has an inhibitory effect on the ability of PolII to travel through the body of the gene.
authors: Zentrum für Medizinische Biotechnologie, Abteilung Genetik, Universität Duisburg-Essen, Essen, Germany.
authors: Franziska
authors: F
authors: Heise
authors: Ho-Ryun
authors: HR
authors: Chung
authors: Jan M
authors: JM
authors: Weber
authors: Zhenyu
authors: Z
authors: Xu
authors: Ludger
authors: L
authors: Klein-Hitpass
authors: Lars M
authors: LM
authors: Steinmetz
authors: Martin
authors: M
authors: Vingron
authors: Ann E
authors: AE
authors: Ehrenhofer-Murray
mesh_terms: D000107:Acetylation; D017353:Gene Deletion; D016681:Genome, Fungal; D051548:Histone Acetyltransferases / Q000235:genetics / Q000378:metabolism*; D006657:Histones / Q000378:metabolism*; D016366:Open Reading Frames; D012441:Saccharomyces cerevisiae / Q000187:drug effects / Q000201:enzymology / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*; D014158:Transcription, Genetic; D014498:Uracil / Q000031:analogs & derivatives / Q000494:pharmacology
chemical_list: D006657:Histones; D029701:Saccharomyces cerevisiae Proteins; D014498:Uracil; D051548:Histone Acetyltransferases; C469266:Sas2 protein, S cerevisiae; C100248:azauracil