Biochemical analysis of the human EVL domains in homologous recombination

Motoki Takaku, Shinichi MacHida, Shugo Nakayama, Daisuke Takahashi, Hitoshi Kurumizaka

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)5841-5848
Number of pages8
JournalFEBS Journal
Volume276
Issue number20
DOIs
Publication statusPublished - 2009 Oct 1

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Keywords

  • DSB
  • ENA/VASP
  • EVL
  • Homologous recombination
  • RAD51

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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