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hCAS/CSE1L regulates RAD51 distribution and focus formation for homologous recombinational repair |
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| Authors: | Satoshi Okimoto Jiying Sun Atsuhiko Fukuto Yasunori Horikoshi Shun Matsuda Tomonari Matsuda Masae Ikura Tsuyoshi Ikura Shinichi Machida Hitoshi Kurumizaka Yoichi Miyamoto Masahiro Oka Yoshihiro Yoneda Yoshiaki Kiuchi Satoshi Tashiro |
| Institution: | 1. Department of Cellular Biology, Research Institute for Radiation Biology and Medicine, Hiroshima University, Hiroshima, Japan;2. Department of Ophthalmology and Visual Science, Graduate School of Biomedical Sciences, Hiroshima University, Hiroshima, Japan;3. Research Center for the Mathematics on Chromatin Live Dynamics, Hiroshima University, Hiroshima, Japan;4. Research Center for Environmental Quality Management, Kyoto University, Otsu, Shiga, Japan;5. Laboratory of Chromatin Regulatory Network, Department of Mutagenesis, Radiation Biology Center, Kyoto University, Yoshida Konoe‐cho, Sakyo‐ku, Kyoto, Japan;6. Laboratory of Structural Biology, Graduate School of Advanced Science and Engineering, Waseda University, 2–2 Wakamatsu‐cho, Shinjuku‐ku, Tokyo, Japan;7. National Institute of Biomedical Innovation, 7–6–8 Saito‐Asagi, Ibaraki, Osaka, Japan |
| Abstract: | Homologous recombinational repair (HR) is one of the major repair systems for DNA double‐strand breaks. RAD51 is a key molecule in HR, and the RAD51 concentration in the cell nucleus increases after DNA damage induction. However, the mechanism that regulates the intracellular distribution of RAD51 is still unclear. Here, we show that hCAS/CSE1L associates with RAD51 in human cells. We found that hCAS/CSE1L negatively regulates the nuclear protein level of RAD51 under normal conditions. hCAS/CSE1L is also required to repress the DNA damage‐induced focus formation of RAD51. Moreover, we show that hCAS/CSE1L plays roles in the regulation of the HR activity and in chromosome stability. These findings suggest that hCAS/CSE1L is responsible for controlling the HR activity by directly interacting with RAD51. |
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