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Contributions of histone tail clipping and acetylation in nucleosome transcription by RNA polymerase II
The N-terminal tails of histones protrude from the nucleosome core and are target sites for histone modifications, such as acetylation and methylation. Histone acetylation is considered to enhance transcription in chromatin. However, the contribution of the histone N-terminal tail to the nucleosome...
Autores principales: | , , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Oxford University Press
2023
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10602921/ https://www.ncbi.nlm.nih.gov/pubmed/37718728 http://dx.doi.org/10.1093/nar/gkad754 |
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author | Oishi, Takumi Hatazawa, Suguru Kujirai, Tomoya Kato, Junko Kobayashi, Yuki Ogasawara, Mitsuo Akatsu, Munetaka Ehara, Haruhiko Sekine, Shun-ichi Hayashi, Gosuke Takizawa, Yoshimasa Kurumizaka, Hitoshi |
author_facet | Oishi, Takumi Hatazawa, Suguru Kujirai, Tomoya Kato, Junko Kobayashi, Yuki Ogasawara, Mitsuo Akatsu, Munetaka Ehara, Haruhiko Sekine, Shun-ichi Hayashi, Gosuke Takizawa, Yoshimasa Kurumizaka, Hitoshi |
author_sort | Oishi, Takumi |
collection | PubMed |
description | The N-terminal tails of histones protrude from the nucleosome core and are target sites for histone modifications, such as acetylation and methylation. Histone acetylation is considered to enhance transcription in chromatin. However, the contribution of the histone N-terminal tail to the nucleosome transcription by RNA polymerase II (RNAPII) has not been clarified. In the present study, we reconstituted nucleosomes lacking the N-terminal tail of each histone, H2A, H2B, H3 or H4, and performed RNAPII transcription assays. We found that the N-terminal tail of H3, but not H2A, H2B and H4, functions in RNAPII pausing at the SHL(-5) position of the nucleosome. Consistently, the RNAPII transcription assay also revealed that the nucleosome containing N-terminally acetylated H3 drastically alleviates RNAPII pausing at the SHL(-5) position. In addition, the H3 acetylated nucleosome produced increased amounts of the run-off transcript. These results provide important evidence that the H3 N-terminal tail plays a role in RNAPII pausing at the SHL(-5) position of the nucleosome, and its acetylation directly alleviates this nucleosome barrier. |
format | Online Article Text |
id | pubmed-10602921 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2023 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-106029212023-10-28 Contributions of histone tail clipping and acetylation in nucleosome transcription by RNA polymerase II Oishi, Takumi Hatazawa, Suguru Kujirai, Tomoya Kato, Junko Kobayashi, Yuki Ogasawara, Mitsuo Akatsu, Munetaka Ehara, Haruhiko Sekine, Shun-ichi Hayashi, Gosuke Takizawa, Yoshimasa Kurumizaka, Hitoshi Nucleic Acids Res Gene regulation, Chromatin and Epigenetics The N-terminal tails of histones protrude from the nucleosome core and are target sites for histone modifications, such as acetylation and methylation. Histone acetylation is considered to enhance transcription in chromatin. However, the contribution of the histone N-terminal tail to the nucleosome transcription by RNA polymerase II (RNAPII) has not been clarified. In the present study, we reconstituted nucleosomes lacking the N-terminal tail of each histone, H2A, H2B, H3 or H4, and performed RNAPII transcription assays. We found that the N-terminal tail of H3, but not H2A, H2B and H4, functions in RNAPII pausing at the SHL(-5) position of the nucleosome. Consistently, the RNAPII transcription assay also revealed that the nucleosome containing N-terminally acetylated H3 drastically alleviates RNAPII pausing at the SHL(-5) position. In addition, the H3 acetylated nucleosome produced increased amounts of the run-off transcript. These results provide important evidence that the H3 N-terminal tail plays a role in RNAPII pausing at the SHL(-5) position of the nucleosome, and its acetylation directly alleviates this nucleosome barrier. Oxford University Press 2023-09-18 /pmc/articles/PMC10602921/ /pubmed/37718728 http://dx.doi.org/10.1093/nar/gkad754 Text en © The Author(s) 2023. Published by Oxford University Press on behalf of Nucleic Acids Research. https://creativecommons.org/licenses/by/4.0/This is an Open Access article distributed under the terms of the Creative Commons Attribution License (https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Gene regulation, Chromatin and Epigenetics Oishi, Takumi Hatazawa, Suguru Kujirai, Tomoya Kato, Junko Kobayashi, Yuki Ogasawara, Mitsuo Akatsu, Munetaka Ehara, Haruhiko Sekine, Shun-ichi Hayashi, Gosuke Takizawa, Yoshimasa Kurumizaka, Hitoshi Contributions of histone tail clipping and acetylation in nucleosome transcription by RNA polymerase II |
title | Contributions of histone tail clipping and acetylation in nucleosome transcription by RNA polymerase II |
title_full | Contributions of histone tail clipping and acetylation in nucleosome transcription by RNA polymerase II |
title_fullStr | Contributions of histone tail clipping and acetylation in nucleosome transcription by RNA polymerase II |
title_full_unstemmed | Contributions of histone tail clipping and acetylation in nucleosome transcription by RNA polymerase II |
title_short | Contributions of histone tail clipping and acetylation in nucleosome transcription by RNA polymerase II |
title_sort | contributions of histone tail clipping and acetylation in nucleosome transcription by rna polymerase ii |
topic | Gene regulation, Chromatin and Epigenetics |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10602921/ https://www.ncbi.nlm.nih.gov/pubmed/37718728 http://dx.doi.org/10.1093/nar/gkad754 |
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