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Methylation of H3 K4 and K79 is not strictly dependent on H2B K123 ubiquitylation

Covalent modifications of histone proteins have profound consequences on chromatin structure and function. Specific modification patterns constitute a code read by effector proteins. Studies from yeast found that H3 trimethylation at K4 and K79 is dependent on ubiquitylation of H2B K123, which is te...

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Detalles Bibliográficos
Autores principales: Foster, Elinor R., Downs, Jessica A.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2009
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2686411/
https://www.ncbi.nlm.nih.gov/pubmed/19255247
http://dx.doi.org/10.1083/jcb.200812088
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author Foster, Elinor R.
Downs, Jessica A.
author_facet Foster, Elinor R.
Downs, Jessica A.
author_sort Foster, Elinor R.
collection PubMed
description Covalent modifications of histone proteins have profound consequences on chromatin structure and function. Specific modification patterns constitute a code read by effector proteins. Studies from yeast found that H3 trimethylation at K4 and K79 is dependent on ubiquitylation of H2B K123, which is termed a “trans-tail pathway.” In this study, we show that a strain unable to be ubiquitylated on H2B (K123R) is still proficient for H3 trimethylation at both K4 and K79, indicating that H3 methylation status is not solely dependent on H2B ubiquitylation. However, additional mutations in H2B result in loss of H3 methylation when combined with htb1-K123R. Consistent with this, we find that the original strain used to identify the trans-tail pathway has a genomic mutation that, when combined with H2B K123R, results in defective H3 methylation. Finally, we show that strains lacking the ubiquitin ligase Bre1 are defective for H3 methylation, suggesting that there is an additional Bre1 substrate that in combination with H2B K123 facilitates H3 methylation.
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spelling pubmed-26864112009-09-09 Methylation of H3 K4 and K79 is not strictly dependent on H2B K123 ubiquitylation Foster, Elinor R. Downs, Jessica A. J Cell Biol Research Articles Covalent modifications of histone proteins have profound consequences on chromatin structure and function. Specific modification patterns constitute a code read by effector proteins. Studies from yeast found that H3 trimethylation at K4 and K79 is dependent on ubiquitylation of H2B K123, which is termed a “trans-tail pathway.” In this study, we show that a strain unable to be ubiquitylated on H2B (K123R) is still proficient for H3 trimethylation at both K4 and K79, indicating that H3 methylation status is not solely dependent on H2B ubiquitylation. However, additional mutations in H2B result in loss of H3 methylation when combined with htb1-K123R. Consistent with this, we find that the original strain used to identify the trans-tail pathway has a genomic mutation that, when combined with H2B K123R, results in defective H3 methylation. Finally, we show that strains lacking the ubiquitin ligase Bre1 are defective for H3 methylation, suggesting that there is an additional Bre1 substrate that in combination with H2B K123 facilitates H3 methylation. The Rockefeller University Press 2009-03-09 /pmc/articles/PMC2686411/ /pubmed/19255247 http://dx.doi.org/10.1083/jcb.200812088 Text en © 2009 Foster and Downs This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).
spellingShingle Research Articles
Foster, Elinor R.
Downs, Jessica A.
Methylation of H3 K4 and K79 is not strictly dependent on H2B K123 ubiquitylation
title Methylation of H3 K4 and K79 is not strictly dependent on H2B K123 ubiquitylation
title_full Methylation of H3 K4 and K79 is not strictly dependent on H2B K123 ubiquitylation
title_fullStr Methylation of H3 K4 and K79 is not strictly dependent on H2B K123 ubiquitylation
title_full_unstemmed Methylation of H3 K4 and K79 is not strictly dependent on H2B K123 ubiquitylation
title_short Methylation of H3 K4 and K79 is not strictly dependent on H2B K123 ubiquitylation
title_sort methylation of h3 k4 and k79 is not strictly dependent on h2b k123 ubiquitylation
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2686411/
https://www.ncbi.nlm.nih.gov/pubmed/19255247
http://dx.doi.org/10.1083/jcb.200812088
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