Recombination activator function of the novel RAD51- and RAD51B-binding protein, human EVL

Motoki Takaku, Shinichi Machida, Noriko Hosoya, Shugo Nakayama, Yoshimasa Takizawa, Isao Sakane, Takehiko Shibata, Kiyoshi Miyagawa, Hitoshi Kurumizaka*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    16 Citations (Scopus)


    The RAD51 protein is a central player in homologous recombinational repair. The RAD51B protein is one of five RAD51 paralogs that function in the homologous recombinational repair pathway in higher eukaryotes. In the present study, we found that the human EVL (Ena/Vasp-like) protein, which is suggested to be involved in actin-remodeling processes, unexpectedly binds to the RAD51 and RAD51B proteins and stimulates the RAD51-mediated homologous pairing and strand exchange. The EVL knockdown cells impaired RAD51 assembly onto damaged DNA after ionizing radiation or mitomycin C treatment. The EVL protein alone promotes single-stranded DNA annealing, and the recombination activities of the EVL protein are further enhanced by the RAD51B protein. The expression of the EVL protein is not ubiquitous, but it is significantly expressed in breast cancer-derived MCF7 cells. These results suggest that the EVL protein is a novel recombination factor that may be required for repairing specific DNA lesions, and that may cause tumor malignancy by its inappropriate expression.

    Original languageEnglish
    Pages (from-to)14326-14336
    Number of pages11
    JournalJournal of Biological Chemistry
    Issue number21
    Publication statusPublished - 2009 May 22

    ASJC Scopus subject areas

    • Biochemistry
    • Cell Biology
    • Molecular Biology


    Dive into the research topics of 'Recombination activator function of the novel RAD51- and RAD51B-binding protein, human EVL'. Together they form a unique fingerprint.

    Cite this