Methylation of H4 lysines 5, 8 and 12 by yeast Set5 calibrates chromatin stress responses

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https://doi.org/10.1038/nsmb.2252
 http://hdl.handle.net/11603/26716

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UMBC Biological Sciences Department

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https://orcid.org/0000-0003-3923-6726

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2012-02-19

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journal articles
postprints
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Green, Erin M et al. “Methylation of H4 lysines 5, 8 and 12 by yeast Set5 calibrates chromatin stress responses.” Nature structural & molecular biology vol. 19,3 361-3. 19 Feb. 2012, doi:10.1038/nsmb.2252

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This version of the article has been accepted for publication, after peer review (when applicable) and is subject to Springer Nature’s AM terms of use, but is not the Version of Record and does not reflect post-acceptance improvements, or any corrections. The Version of Record is available online at: http://dx.doi.org/10.1038/nsmb.2252

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Abstract

Methylation of histones is central to chromatin regulation, and thus novel mechanisms regulating genome function can be revealed through the discovery of new histone methyl marks. Here, we identify Set5 as the first histone H4 methyltransferase in budding yeast, which monomethylates the important H4 lysine residues 5, 8 and 12. Set5’s enzymatic activity functions together with the global chromatin-modifying complexes COMPASS and NuA4 to regulate cell growth and stress responses.