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Histone H2B ubiquitylation and H3 lysine 4 methylation prevent ectopic silencing of euchromatic loci important for the cellular response to heat

In Saccharomyces cerevisiae, ubiquitylation of histone H2B signals methylation of histone H3 at lysine residues 4 (K4) and 79. These modifications occur at active genes but are believed to stabilize silent chromatin by limiting movement of silencing proteins away from heterochromatin domains. In the...

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Autores principales: Leung, Amy, Cajigas, Ivelisse, Jia, Peilin, Ezhkova, Elena, Brickner, Jason H., Zhao, Zhongming, Geng, Fuqiang, Tansey, William P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The American Society for Cell Biology 2011
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3145549/
https://www.ncbi.nlm.nih.gov/pubmed/21680712
http://dx.doi.org/10.1091/mbc.E11-05-0426
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author Leung, Amy
Cajigas, Ivelisse
Jia, Peilin
Ezhkova, Elena
Brickner, Jason H.
Zhao, Zhongming
Geng, Fuqiang
Tansey, William P.
author_facet Leung, Amy
Cajigas, Ivelisse
Jia, Peilin
Ezhkova, Elena
Brickner, Jason H.
Zhao, Zhongming
Geng, Fuqiang
Tansey, William P.
author_sort Leung, Amy
collection PubMed
description In Saccharomyces cerevisiae, ubiquitylation of histone H2B signals methylation of histone H3 at lysine residues 4 (K4) and 79. These modifications occur at active genes but are believed to stabilize silent chromatin by limiting movement of silencing proteins away from heterochromatin domains. In the course of studying atypical phenotypes associated with loss of H2B ubiquitylation/H3K4 methylation, we discovered that these modifications are also required for cell wall integrity at high temperatures. We identified the silencing protein Sir4 as a dosage suppressor of loss of H2B ubiquitylation, and we showed that elevated Sir4 expression suppresses cell wall integrity defects by inhibiting the function of the Sir silencing complex. Using comparative transcriptome analysis, we identified a set of euchromatic genes—enriched in those required for the cellular response to heat—whose expression is attenuated by loss of H2B ubiquitylation but restored by disruption of Sir function. Finally, using DNA adenine methyltransferase identification, we found that Sir3 and Sir4 associate with genes that are silenced in the absence of H3K4 methylation. Our data reveal that H2B ubiquitylation/H3K4 methylation play an important role in limiting ectopic association of silencing proteins with euchromatic genes important for cell wall integrity and the response to heat.
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spelling pubmed-31455492011-10-16 Histone H2B ubiquitylation and H3 lysine 4 methylation prevent ectopic silencing of euchromatic loci important for the cellular response to heat Leung, Amy Cajigas, Ivelisse Jia, Peilin Ezhkova, Elena Brickner, Jason H. Zhao, Zhongming Geng, Fuqiang Tansey, William P. Mol Biol Cell Articles In Saccharomyces cerevisiae, ubiquitylation of histone H2B signals methylation of histone H3 at lysine residues 4 (K4) and 79. These modifications occur at active genes but are believed to stabilize silent chromatin by limiting movement of silencing proteins away from heterochromatin domains. In the course of studying atypical phenotypes associated with loss of H2B ubiquitylation/H3K4 methylation, we discovered that these modifications are also required for cell wall integrity at high temperatures. We identified the silencing protein Sir4 as a dosage suppressor of loss of H2B ubiquitylation, and we showed that elevated Sir4 expression suppresses cell wall integrity defects by inhibiting the function of the Sir silencing complex. Using comparative transcriptome analysis, we identified a set of euchromatic genes—enriched in those required for the cellular response to heat—whose expression is attenuated by loss of H2B ubiquitylation but restored by disruption of Sir function. Finally, using DNA adenine methyltransferase identification, we found that Sir3 and Sir4 associate with genes that are silenced in the absence of H3K4 methylation. Our data reveal that H2B ubiquitylation/H3K4 methylation play an important role in limiting ectopic association of silencing proteins with euchromatic genes important for cell wall integrity and the response to heat. The American Society for Cell Biology 2011-08-01 /pmc/articles/PMC3145549/ /pubmed/21680712 http://dx.doi.org/10.1091/mbc.E11-05-0426 Text en © 2011 Leung et al. This article is distributed by The American Society for Cell Biology under license from the author(s). Two months after publication it is available to the public under an Attribution–Noncommercial–Share Alike 3.0 Unported Creative Commons License (http://creativecommons.org/licenses/by-nc-sa/3.0). “ASCB®,” “The American Society for Cell Biology®,” and “Molecular Biology of the Cell®” are registered trademarks of The American Society of Cell Biology.
spellingShingle Articles
Leung, Amy
Cajigas, Ivelisse
Jia, Peilin
Ezhkova, Elena
Brickner, Jason H.
Zhao, Zhongming
Geng, Fuqiang
Tansey, William P.
Histone H2B ubiquitylation and H3 lysine 4 methylation prevent ectopic silencing of euchromatic loci important for the cellular response to heat
title Histone H2B ubiquitylation and H3 lysine 4 methylation prevent ectopic silencing of euchromatic loci important for the cellular response to heat
title_full Histone H2B ubiquitylation and H3 lysine 4 methylation prevent ectopic silencing of euchromatic loci important for the cellular response to heat
title_fullStr Histone H2B ubiquitylation and H3 lysine 4 methylation prevent ectopic silencing of euchromatic loci important for the cellular response to heat
title_full_unstemmed Histone H2B ubiquitylation and H3 lysine 4 methylation prevent ectopic silencing of euchromatic loci important for the cellular response to heat
title_short Histone H2B ubiquitylation and H3 lysine 4 methylation prevent ectopic silencing of euchromatic loci important for the cellular response to heat
title_sort histone h2b ubiquitylation and h3 lysine 4 methylation prevent ectopic silencing of euchromatic loci important for the cellular response to heat
topic Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3145549/
https://www.ncbi.nlm.nih.gov/pubmed/21680712
http://dx.doi.org/10.1091/mbc.E11-05-0426
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