https://scholars.lib.ntu.edu.tw/handle/123456789/634920
標題: | A RAD51-ADP double filament structure unveils the mechanism of filament dynamics in homologous recombination | 作者: | Luo, Shih-Chi Yeh, Min-Chi Lien, Yu-Hsiang Yeh, Hsin-Yi Siao, Huei-Lun Tu, I-Ping HUNG-YUAN CHI Ho, Meng-Chiao |
公開日期: | 17-八月-2023 | 出版社: | Nature Research | 卷: | 14 | 期: | 1 | 起(迄)頁: | Article number 4993 | 來源出版物: | Nature communications | 摘要: | ATP-dependent RAD51 recombinases play an essential role in eukaryotic homologous recombination by catalyzing a four-step process: 1) formation of a RAD51 single-filament assembly on ssDNA in the presence of ATP, 2) complementary DNA strand-exchange, 3) ATP hydrolysis transforming the RAD51 filament into an ADP-bound disassembly-competent state, and 4) RAD51 disassembly to provide access for DNA repairing enzymes. Of these steps, filament dynamics between the ATP- and ADP-bound states, and the RAD51 disassembly mechanism, are poorly understood due to the lack of near-atomic-resolution information of the ADP-bound RAD51-DNA filament structure. We report the cryo-EM structure of ADP-bound RAD51-DNA filaments at 3.1 Å resolution, revealing a unique RAD51 double-filament that wraps around ssDNA. Structural analysis, supported by ATP-chase and time-resolved cryo-EM experiments, reveals a collapsing mechanism involving two four-protomer movements along ssDNA for mechanical transition between RAD51 single- and double-filament without RAD51 dissociation. This mechanism enables elastic change of RAD51 filament length during structural transitions between ATP- and ADP-states. |
URI: | https://scholars.lib.ntu.edu.tw/handle/123456789/634920 | ISSN: | 2041-1723 | DOI: | 10.1038/s41467-023-40672-5 |
顯示於: | 生化科學研究所 |
在 IR 系統中的文件,除了特別指名其著作權條款之外,均受到著作權保護,並且保留所有的權利。