Mechanistic insights into RAD51-associated protein 1 (RAD51AP1) action in homologous DNA repair |
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Authors: | Dunlop Myun Hwa Dray Eloïse Zhao Weixing San Filippo Joseph Tsai Miaw-Sheue Leung Stanley G Schild David Wiese Claudia Sung Patrick |
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Affiliation: | Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA. |
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Abstract: | Homologous recombination catalyzed by the RAD51 recombinase is essential for maintaining genome integrity upon the induction of DNA double strand breaks and other DNA lesions. By enhancing the recombinase activity of RAD51, RAD51AP1 (RAD51-associated protein 1) serves a key role in homologous recombination-mediated chromosome damage repair. We show here that RAD51AP1 harbors two distinct DNA binding domains that are both needed for maximal protein activity under physiological conditions. We have finely mapped the two DNA binding domains in RAD51AP1 and generated mutant variants that are impaired in either or both of the DNA binding domains. Examination of these mutants reveals that both domains are indispensable for RAD51AP1 function in cells. These and other results illuminate the mechanistic basis of RAD51AP1 action in homologous DNA repair. |
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Keywords: | DNA-binding protein DNA Recombination DNA Repair DNA-Protein Interaction Homologous Recombination RAD51 RAD51AP1 |
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