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

Myun Hwa Dunlop, Eloïse Dray, Weixing Zhao, Joseph San Filippo, Miaw Sheue Tsai, Stanley G. Leung, David Schild, Claudia Wiese, Patrick Sung

Research output: Contribution to journalArticle

19 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)12343-12347
Number of pages5
JournalJournal of Biological Chemistry
Volume287
Issue number15
DOIs
StatePublished - Apr 6 2012
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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