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Biochemical analysis of the human EVL domains in homologous recombination
Author(s) -
Takaku Motoki,
Machida Shinichi,
Nakayama Shugo,
Takahashi Daisuke,
Kurumizaka Hitoshi
Publication year - 2009
Publication title -
the febs journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.981
H-Index - 204
eISSN - 1742-4658
pISSN - 1742-464X
DOI - 10.1111/j.1742-4658.2009.07265.x
Subject(s) - rad51 , homologous recombination , biology , homologous chromosome , uniprot , recombination , dna , genetics , microbiology and biotechnology , non homologous end joining , function (biology) , gene
EVL is a member of the ENA/VASP family, which is involved in actin‐remodeling processes. Previously, we reported that human EVL directly interacts with RAD51, which is an essential protein in the homologous recombinational repair of DNA double‐strand breaks, and stimulates RAD51‐mediated recombination reactions in vitro . To identify the EVL domain required for the recombination function, we purified the EVL fragments EVL(1–221) and EVL(222–418), which contain the EVH1 and Pro‐rich domains and the EVH2 domain, respectively. We found that EVL(222–418) possesses DNA‐binding and RAD51‐binding activities, and also stimulates RAD51‐mediated homologous pairing. In contrast, EVL(1–221) did not exhibit any of these activities. Therefore, the EVH2 domain, which is highly conserved among the ENA/VASP family proteins, may be responsible for the recombination function of EVL. Structured digital abstract• MINT‐7239394 : EVL (uniprotkb: Q9UI08 ) binds ( MI:0407 ) to RAD51 (uniprotkb: Q06609 ) by pull down ( MI:0096 )