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Replication-independent nucleosome exchange is enhanced by local and specific acetylation of histone H4

We used a novel single-cell strategy to examine the fate of histones during G(2)-phase. Consistent with previous results, we find that in G(2)-phase, the majority of nuclear histones are assembled into chromatin, whereas a small fraction comprises an unassembled pool. Small increases in the amount o...

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Autores principales: Elliott, Giles O., Murphy, Kevin J., Hayes, Jeffrey J., Thiriet, Christophe
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Oxford University Press 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3575802/
https://www.ncbi.nlm.nih.gov/pubmed/23303778
http://dx.doi.org/10.1093/nar/gks1451
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author Elliott, Giles O.
Murphy, Kevin J.
Hayes, Jeffrey J.
Thiriet, Christophe
author_facet Elliott, Giles O.
Murphy, Kevin J.
Hayes, Jeffrey J.
Thiriet, Christophe
author_sort Elliott, Giles O.
collection PubMed
description We used a novel single-cell strategy to examine the fate of histones during G(2)-phase. Consistent with previous results, we find that in G(2)-phase, the majority of nuclear histones are assembled into chromatin, whereas a small fraction comprises an unassembled pool. Small increases in the amount of histones within the free pool affect the extent of exchange, suggesting that the free pool is in dynamic equilibrium with chromatin proteins. Unexpectedly, acetylated H4 is preferentially partitioned to the unassembled pool. Although an increase in global histone acetylation did not affect overall nucleosome dynamics, an H4 containing lysine to glutamine substitutions as mimics of acetylation significantly increased the rate of exchange, but did not affect the acetylation state of neighbouring nucleosomes. Interestingly, transcribed regions are particularly predisposed to exchange on incorporation of H4 acetylation mimics compared with surrounding regions. Our results support a model whereby histone acetylation on K8 and K16 specifically marks nucleosomes for eviction, with histones being rapidly deacetylated on reassembly.
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spelling pubmed-35758022013-02-19 Replication-independent nucleosome exchange is enhanced by local and specific acetylation of histone H4 Elliott, Giles O. Murphy, Kevin J. Hayes, Jeffrey J. Thiriet, Christophe Nucleic Acids Res Gene Regulation, Chromatin and Epigenetics We used a novel single-cell strategy to examine the fate of histones during G(2)-phase. Consistent with previous results, we find that in G(2)-phase, the majority of nuclear histones are assembled into chromatin, whereas a small fraction comprises an unassembled pool. Small increases in the amount of histones within the free pool affect the extent of exchange, suggesting that the free pool is in dynamic equilibrium with chromatin proteins. Unexpectedly, acetylated H4 is preferentially partitioned to the unassembled pool. Although an increase in global histone acetylation did not affect overall nucleosome dynamics, an H4 containing lysine to glutamine substitutions as mimics of acetylation significantly increased the rate of exchange, but did not affect the acetylation state of neighbouring nucleosomes. Interestingly, transcribed regions are particularly predisposed to exchange on incorporation of H4 acetylation mimics compared with surrounding regions. Our results support a model whereby histone acetylation on K8 and K16 specifically marks nucleosomes for eviction, with histones being rapidly deacetylated on reassembly. Oxford University Press 2013-02 2013-01-07 /pmc/articles/PMC3575802/ /pubmed/23303778 http://dx.doi.org/10.1093/nar/gks1451 Text en © The Author(s) 2013. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Gene Regulation, Chromatin and Epigenetics
Elliott, Giles O.
Murphy, Kevin J.
Hayes, Jeffrey J.
Thiriet, Christophe
Replication-independent nucleosome exchange is enhanced by local and specific acetylation of histone H4
title Replication-independent nucleosome exchange is enhanced by local and specific acetylation of histone H4
title_full Replication-independent nucleosome exchange is enhanced by local and specific acetylation of histone H4
title_fullStr Replication-independent nucleosome exchange is enhanced by local and specific acetylation of histone H4
title_full_unstemmed Replication-independent nucleosome exchange is enhanced by local and specific acetylation of histone H4
title_short Replication-independent nucleosome exchange is enhanced by local and specific acetylation of histone H4
title_sort replication-independent nucleosome exchange is enhanced by local and specific acetylation of histone h4
topic Gene Regulation, Chromatin and Epigenetics
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3575802/
https://www.ncbi.nlm.nih.gov/pubmed/23303778
http://dx.doi.org/10.1093/nar/gks1451
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