Mechanistic insights into RAD51-associated protein 1 (RAD51AP1) action in homologous DNA repair

Dunlop, Myun Hwa, Dray, Eloise, Zhao, Weixing, San Filippo, Joseph, Tsai, Miaw-Sheue, Leung, Stanley G., Schild, David, Wiese, Claudia, & Sung, Patrick (2012) Mechanistic insights into RAD51-associated protein 1 (RAD51AP1) action in homologous DNA repair. Journal of Biological Chemistry, 287(15), pp. 12343-12347.

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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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9 citations in Web of Science®

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ID Code: 73270
Item Type: Journal Article
Refereed: Yes
Additional Information: Articles free to read on journal website after 12 months
DOI: 10.1074/jbc.C112.352161
ISSN: 1083-351X
Subjects: Australian and New Zealand Standard Research Classification > MEDICAL AND HEALTH SCIENCES (110000) > MEDICAL BIOCHEMISTRY AND METABOLOMICS (110100)
Australian and New Zealand Standard Research Classification > MEDICAL AND HEALTH SCIENCES (110000) > MEDICAL MICROBIOLOGY (110800)
Divisions: Current > Schools > School of Biomedical Sciences
Current > QUT Faculties and Divisions > Faculty of Health
Current > Institutes > Institute of Health and Biomedical Innovation
Deposited On: 02 Jul 2014 23:19
Last Modified: 04 Feb 2015 05:38

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