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  Genome-wide H4 K16 acetylation by SAS-I is deposited independently of transcription and histone exchange

Heise, F., Chung, H.-R., Weber, J. M., Xu, Z., Klein-Hitpass, L., Steinmetz, L. M., et al. (2012). Genome-wide H4 K16 acetylation by SAS-I is deposited independently of transcription and histone exchange. Nucleic Acids Research (London), 40(1), 65-74. doi:10.1093/nar/gkr649.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-E87E-7 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-000E-E87F-5
Genre: Journal Article

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© 2011 Oxford University Press
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 Creators:
Heise, Franziska1, Author
Chung, Ho-Ryun2, Author              
Weber, Jan M.1, Author
Xu, Zhenyu3, Author
Klein-Hitpass, Ludger4, Author
Steinmetz, Lars M.3, Author
Vingron, Martin5, Author              
Ehrenhofer-Murray, Ann E.1, Author
Affiliations:
1Zentrum für Medizinische Biotechnologie, Abteilung Genetik, Universität Duisburg-Essen, Essen, Germany, ou_persistent22              
2Computational Epigenetics (Ho-Ryun Chung), Independent Junior Research Groups (OWL), Max Planck Institute for Molecular Genetics, Max Planck Society, Berlin, Germany, ou_1479658              
3European Molecular Biology Laboratory, Meyerhofstraße 1, Heidelberg, Germany, ou_persistent22              
4Institut für Zellbiologie, Universitätsklinikum Essen, Essen, Germany, ou_persistent22              
5Gene regulation (Martin Vingron), Dept. of Computational Molecular Biology (Head: Martin Vingron), Max Planck Institute for Molecular Genetics, Max Planck Society, ou_1479639              

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 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 sas2Delta 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 sas2Delta, indicating that Sas2 deposited this modification on chromatin independently of histone exchange. In agreement with the effect of Sas2 within ORFs, sas2Delta 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.

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Language(s): eng - English
 Dates: 2011-09-092012
 Publication Status: Published in print
 Pages: -
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 Rev. Method: Peer
 Identifiers: DOI: 10.1093/nar/gkr649
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Title: Nucleic Acids Research (London)
  Other : Nucleic Acids Res
Source Genre: Journal
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Publ. Info: Oxford : Oxford University Press
Pages: - Volume / Issue: 40 (1) Sequence Number: - Start / End Page: 65 - 74 Identifier: ISSN: 0305-1048
CoNE: /journals/resource/110992357379342