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Histone H3 N-terminal acetylation sites especially K14 are important for rDNA silencing and aging
Histone variants and histone modifications are essential components in the establishment and maintenance of the repressed status of heterochromatin. Among these histone variants and modifications, acetylation at histone H4K16 is uniquely important for the maintenance of silencing at telomere and mat...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Nature Publishing Group
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4764821/ https://www.ncbi.nlm.nih.gov/pubmed/26906758 http://dx.doi.org/10.1038/srep21900 |
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author | Xu, Heng-hao Su, Trent Xue, Yong |
author_facet | Xu, Heng-hao Su, Trent Xue, Yong |
author_sort | Xu, Heng-hao |
collection | PubMed |
description | Histone variants and histone modifications are essential components in the establishment and maintenance of the repressed status of heterochromatin. Among these histone variants and modifications, acetylation at histone H4K16 is uniquely important for the maintenance of silencing at telomere and mating type loci but not at the ribosomal DNA locus. Here we show that mutations at H3 N-terminal acetylation site K14 specifically disrupt rDNA silencing. However, the mutant ion at H3K14R doesn’t affect the recruitment of Pol II repressor RENT (regulator of nucleolar silencing and telophase exit) complex at the rDNA region. Instead, the CAF-1(chromatin assembly factor I) subunit Cac2 level decreased in the H3K14R mutant. Further experiments revealed that the single mutation at H3K14 and multi-site mutations at H3 N-terminus including K14 also delayed replication-depend nucleosome assembly and advanced replicative life span. In conclusion, our data suggest that histone H3 N-terminal acetylation sites especially at K14 are important for rDNA silencing and aging. |
format | Online Article Text |
id | pubmed-4764821 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Nature Publishing Group |
record_format | MEDLINE/PubMed |
spelling | pubmed-47648212016-03-02 Histone H3 N-terminal acetylation sites especially K14 are important for rDNA silencing and aging Xu, Heng-hao Su, Trent Xue, Yong Sci Rep Article Histone variants and histone modifications are essential components in the establishment and maintenance of the repressed status of heterochromatin. Among these histone variants and modifications, acetylation at histone H4K16 is uniquely important for the maintenance of silencing at telomere and mating type loci but not at the ribosomal DNA locus. Here we show that mutations at H3 N-terminal acetylation site K14 specifically disrupt rDNA silencing. However, the mutant ion at H3K14R doesn’t affect the recruitment of Pol II repressor RENT (regulator of nucleolar silencing and telophase exit) complex at the rDNA region. Instead, the CAF-1(chromatin assembly factor I) subunit Cac2 level decreased in the H3K14R mutant. Further experiments revealed that the single mutation at H3K14 and multi-site mutations at H3 N-terminus including K14 also delayed replication-depend nucleosome assembly and advanced replicative life span. In conclusion, our data suggest that histone H3 N-terminal acetylation sites especially at K14 are important for rDNA silencing and aging. Nature Publishing Group 2016-02-24 /pmc/articles/PMC4764821/ /pubmed/26906758 http://dx.doi.org/10.1038/srep21900 Text en Copyright © 2016, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/ |
spellingShingle | Article Xu, Heng-hao Su, Trent Xue, Yong Histone H3 N-terminal acetylation sites especially K14 are important for rDNA silencing and aging |
title | Histone H3 N-terminal acetylation sites especially K14 are important for rDNA silencing and aging |
title_full | Histone H3 N-terminal acetylation sites especially K14 are important for rDNA silencing and aging |
title_fullStr | Histone H3 N-terminal acetylation sites especially K14 are important for rDNA silencing and aging |
title_full_unstemmed | Histone H3 N-terminal acetylation sites especially K14 are important for rDNA silencing and aging |
title_short | Histone H3 N-terminal acetylation sites especially K14 are important for rDNA silencing and aging |
title_sort | histone h3 n-terminal acetylation sites especially k14 are important for rdna silencing and aging |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4764821/ https://www.ncbi.nlm.nih.gov/pubmed/26906758 http://dx.doi.org/10.1038/srep21900 |
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