Literature DB >> 19725871

Biochemical analysis of the human EVL domains in homologous recombination.

Motoki Takaku1, Shinichi Machida, Shugo Nakayama, Daisuke Takahashi, Hitoshi Kurumizaka.   

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. Structured digital abstract: * MINT-7239394: EVL (uniprotkb:Q9UI08) binds (MI:0407) to RAD51 (uniprotkb:Q06609) by pull down (MI:0096).

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Year:  2009        PMID: 19725871     DOI: 10.1111/j.1742-4658.2009.07265.x

Source DB:  PubMed          Journal:  FEBS J        ISSN: 1742-464X            Impact factor:   5.542


  1 in total

1.  Single-stranded DNA catenation mediated by human EVL and a type I topoisomerase.

Authors:  Motoki Takaku; Daisuke Takahashi; Shinichi Machida; Hiroyuki Ueno; Noriko Hosoya; Shukuko Ikawa; Kiyoshi Miyagawa; Takehiko Shibata; Hitoshi Kurumizaka
Journal:  Nucleic Acids Res       Date:  2010-07-17       Impact factor: 16.971

  1 in total

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