Heise, Franziska; Chung, Ho-Ryun; Weber, Jan; Xu, Zhenyu; Klein-Hitpaß, Ludger; Steinmetz, Lars M.; Vingron, Martin; Ehrenhofer-Murray, Ann:
Genome-wide H4 K16 acetylation by SAS-I is deposited independently of transcription and histone exchange
In: Nucleic Acids Research, Vol. 40 (2012), No. 1, pp. 65 - 74
2012article/chapter in journalOA Embargo
BiologyMedicineScientific institutes » Center of Medical Biotechnology (ZMB) Faculty of Medicine » Essen University Hospital » Institute of Cell Biology (Tumor Research)
Related: 1 publication(s)
Title in English:
Genome-wide H4 K16 acetylation by SAS-I is deposited independently of transcription and histone exchange
Author:
Heise, FranziskaUDE
LSF ID
51869
Other
connected with university
;
Chung, Ho-Ryun;Weber, JanUDE
LSF ID
17095
Other
connected with university
;
Xu, Zhenyu;Klein-Hitpaß, LudgerUDE
LSF ID
14385
ORCID
0000-0002-6406-8376ORCID iD
Other
connected with university
;
Steinmetz, Lars M.;Vingron, Martin;Ehrenhofer-Murray, AnnUDE
LSF ID
12062
Other
connected with university
Year of publication:
2012
Open Access?:
OA Embargo
EVALuna Biblio ID
19105
Web of Science ID
PubMed ID
Scopus ID
Language of text:
English

Abstract in English:

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.