Identification of a second DNA binding site in the human Rad52 protein

Wataru Kagawa, Ako Kagawa, Kengo Saito, Shukuko Ikawa, Takehiko Shibata, Hitoshi Kurumizaka*, Shigeyuki Yokoyama


    研究成果: Article査読

    47 被引用数 (Scopus)


    Rad52 plays essential roles in homology-dependent double-strand break repair. Various studies have established the functions of Rad52 in Rad51-dependent and Rad51-independent repair processes. However, the precise molecular mechanisms of Rad52 in these processes remain unknown. In the present study we have identified a novel DNA binding site within Rad52 by a structure-based alanine scan mutagenesis. This site is closely aligned with the putative single-stranded DNA binding site determined previously. Mutations in this site impaired the ability of the Rad52-single-stranded DNA complex to form a ternary complex with double-stranded DNA and subsequently catalyze the formation of D-loops. We found that Rad52 introduces positive supercoils into double-stranded DNA and that the second DNA binding site is essential for this activity. Our findings suggest that Rad52 aligns two recombining DNA molecules within the first and second DNA binding sites to stimulate the homology search and strand invasion processes.

    ジャーナルJournal of Biological Chemistry
    出版ステータスPublished - 2008 8 29

    ASJC Scopus subject areas

    • 生化学
    • 細胞生物学
    • 分子生物学


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