| Title | Yeast Bromodomain Factor 1 and Its Human Homolog TAF1 Play Conserved Roles in Promoting Homologous Recombination |
| Authors | 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 |
| Affiliation | Wuhan Univ, Coll Life Sci, Hubei Key Lab Cell Homeostasis, Wuhan 430072, Peoples R China Wuhan Univ, Inst Adv Studies, Wuhan 430072, Peoples R China George Washington Univ, Dept Biochem & Mol Med, Sch Med & Hlth Sci, Washington, DC 20037 USA Peking Univ, Sch Life Sci, State Key Lab Prot & Plant Gene Res, Beijing 100871, Peoples R China Peking Univ, Peking Tsinghua Ctr Life Sci, Beijing 100871, Peoples R China |
| Keywords | SINGLE-STRANDED-DNA REPLICATION PROTEIN-A HISTONE H4 SACCHAROMYCES-CEREVISIAE NUCLEOSOME-LIKE END-RESECTION DAMAGE COMPLEXES DYNAMICS REPAIR |
| Issue Date | May-2021 |
| Publisher | ADVANCED SCIENCE |
| Abstract | 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. |
| URI | http://hdl.handle.net/20.500.11897/614534 |
| DOI | 10.1002/advs.202100753 |
| Indexed | SCI(E) |
| Appears in Collections: | 生命科学学院 |
