Host: The Japan Radiation Research Society, Chairman of the 52nd Annual Meeting, Toshiteru Okubo (Radiation Effects Research Foundation)
53BP1 is rapidly recruited at sites of DNA double-strand breaks (DSBs) after treatment of cells with ionizing radiation or DNA-damaging agents, and is suggested to be involved in DNA damage checkpoint and DNA repair. Recently, the molecular mechanism of the recruitment of 53BP1 to DSB-sites has been revealed. In contrast, molecular bases for the functions of 53BP1, including regulation of DNA damage checkpoint and DNA repair, are still unclear. To investigate molecular mechanisms of 53BP1 function after the recruitment of 53BP1 to DSB-sites, we attempted to identify proteins which bind to the BRCT domain of 53BP1. The C-terminal region of 53BP1, including the nuclear localization signal and the BRCT domain, was fused downstream of the FLAG-HA tag and expressed in U2OS cells. The proteins co-immunoprecipitated with the FLAG-HA-BRCT protein were analyzed. We will show the results and discuss the molecular mechanism of 53BP1 in this meeting.
