Related Experiment Video
Updated: May 24, 2026

Real-time Observation of the DNA Strand Exchange Reaction Mediated by Rad51
Published on: February 13, 2019
Mechanistic insights into RAD51-associated protein 1 (RAD51AP1) action in homologous DNA repair
Myun Hwa Dunlop1, Eloïse Dray, Weixing Zhao
1Department of Molecular Biophysics and Biochemistry, Yale University School of Medicine, New Haven, Connecticut 06520, USA.
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.
Related Concept Videos
Homologous Recombination
Restarting Stalled Replication Forks
DNA Damage can Stall the Cell Cycle
DNA Damage Can Stall the Cell Cycle
Long-patch Base Excision Repair
Fixing Double-strand Breaks

