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Yeast Bromodomain Factor 1 and Its Human Homolog TAF1 Play Conserved Roles in Promoting Homologous Recombination

Histone acetylation is a key histone post‐translational modification that shapes chromatin structure, dynamics, and function. Bromodomain (BRD) proteins, the readers of acetyl‐lysines, are located in the center of the histone acetylation‐signaling network. How they regulate DNA repair and genome sta...

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Autores principales: Peng, Haoyang, Zhang, Simin, Peng, Yihan, Zhu, Shuangyi, Zhao, Xin, Zhao, Xiaocong, Yang, Shuangshuang, Liu, Guangxue, Dong, Yang, Gan, Xiaoli, Li, Qing, Zhang, Xinghua, Pei, Huadong, Chen, Xuefeng
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8336524/
https://www.ncbi.nlm.nih.gov/pubmed/34056863
http://dx.doi.org/10.1002/advs.202100753
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author Peng, Haoyang
Zhang, Simin
Peng, Yihan
Zhu, Shuangyi
Zhao, Xin
Zhao, Xiaocong
Yang, Shuangshuang
Liu, Guangxue
Dong, Yang
Gan, Xiaoli
Li, Qing
Zhang, Xinghua
Pei, Huadong
Chen, Xuefeng
author_facet Peng, Haoyang
Zhang, Simin
Peng, Yihan
Zhu, Shuangyi
Zhao, Xin
Zhao, Xiaocong
Yang, Shuangshuang
Liu, Guangxue
Dong, Yang
Gan, Xiaoli
Li, Qing
Zhang, Xinghua
Pei, Huadong
Chen, Xuefeng
author_sort Peng, Haoyang
collection PubMed
description Histone acetylation is a key histone post‐translational modification that shapes chromatin structure, dynamics, and function. Bromodomain (BRD) proteins, the readers of acetyl‐lysines, are located in the center of the histone acetylation‐signaling network. How they regulate DNA repair and genome stability remains poorly understood. Here, a conserved function of the yeast Bromodomain Factor 1 (Bdf1) and its human counterpart TAF1 is reported in promoting DNA double‐stranded break repair by homologous recombination (HR). Depletion of either yeast BDF1 or human TAF1, or disruption of their BRDs impairs DNA end resection, Replication Protein A (RPA) and Rad51 loading, and HR repair, causing genome instability and hypersensitivity to DNA damage. Mechanistically, it is shown that Bdf1 preferentially binds the DNA damage‐induced histone H4 acetylation (H4Ac) via the BRD motifs, leading to its chromatin recruitment. Meanwhile, Bdf1 physically interacts with RPA, and this interaction facilitates RPA loading in the chromatin context and the subsequent HR repair. Similarly, TAF1 also interacts with H4Ac or RPA. Thus, Bdf1 and TAF1 appear to share a conserved mechanism in linking the HR repair to chromatin acetylation in preserving genome integrity.
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spelling pubmed-83365242021-08-09 Yeast Bromodomain Factor 1 and Its Human Homolog TAF1 Play Conserved Roles in Promoting Homologous Recombination Peng, Haoyang Zhang, Simin Peng, Yihan Zhu, Shuangyi Zhao, Xin Zhao, Xiaocong Yang, Shuangshuang Liu, Guangxue Dong, Yang Gan, Xiaoli Li, Qing Zhang, Xinghua Pei, Huadong Chen, Xuefeng Adv Sci (Weinh) Research Articles Histone acetylation is a key histone post‐translational modification that shapes chromatin structure, dynamics, and function. Bromodomain (BRD) proteins, the readers of acetyl‐lysines, are located in the center of the histone acetylation‐signaling network. How they regulate DNA repair and genome stability remains poorly understood. Here, a conserved function of the yeast Bromodomain Factor 1 (Bdf1) and its human counterpart TAF1 is reported in promoting DNA double‐stranded break repair by homologous recombination (HR). Depletion of either yeast BDF1 or human TAF1, or disruption of their BRDs impairs DNA end resection, Replication Protein A (RPA) and Rad51 loading, and HR repair, causing genome instability and hypersensitivity to DNA damage. Mechanistically, it is shown that Bdf1 preferentially binds the DNA damage‐induced histone H4 acetylation (H4Ac) via the BRD motifs, leading to its chromatin recruitment. Meanwhile, Bdf1 physically interacts with RPA, and this interaction facilitates RPA loading in the chromatin context and the subsequent HR repair. Similarly, TAF1 also interacts with H4Ac or RPA. Thus, Bdf1 and TAF1 appear to share a conserved mechanism in linking the HR repair to chromatin acetylation in preserving genome integrity. John Wiley and Sons Inc. 2021-05-30 /pmc/articles/PMC8336524/ /pubmed/34056863 http://dx.doi.org/10.1002/advs.202100753 Text en © 2021 The Authors. Advanced Science published by Wiley‐VCH GmbH https://creativecommons.org/licenses/by/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Research Articles
Peng, Haoyang
Zhang, Simin
Peng, Yihan
Zhu, Shuangyi
Zhao, Xin
Zhao, Xiaocong
Yang, Shuangshuang
Liu, Guangxue
Dong, Yang
Gan, Xiaoli
Li, Qing
Zhang, Xinghua
Pei, Huadong
Chen, Xuefeng
Yeast Bromodomain Factor 1 and Its Human Homolog TAF1 Play Conserved Roles in Promoting Homologous Recombination
title Yeast Bromodomain Factor 1 and Its Human Homolog TAF1 Play Conserved Roles in Promoting Homologous Recombination
title_full Yeast Bromodomain Factor 1 and Its Human Homolog TAF1 Play Conserved Roles in Promoting Homologous Recombination
title_fullStr Yeast Bromodomain Factor 1 and Its Human Homolog TAF1 Play Conserved Roles in Promoting Homologous Recombination
title_full_unstemmed Yeast Bromodomain Factor 1 and Its Human Homolog TAF1 Play Conserved Roles in Promoting Homologous Recombination
title_short Yeast Bromodomain Factor 1 and Its Human Homolog TAF1 Play Conserved Roles in Promoting Homologous Recombination
title_sort yeast bromodomain factor 1 and its human homolog taf1 play conserved roles in promoting homologous recombination
topic Research Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8336524/
https://www.ncbi.nlm.nih.gov/pubmed/34056863
http://dx.doi.org/10.1002/advs.202100753
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