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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...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2013
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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. |
format | Online Article Text |
id | pubmed-3575802 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2013 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
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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