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

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    55 Citations (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.

    Original languageEnglish
    Pages (from-to)24264-24273
    Number of pages10
    JournalJournal of Biological Chemistry
    Issue number35
    Publication statusPublished - 2008 Aug 29

    ASJC Scopus subject areas

    • Biochemistry
    • Cell Biology
    • Molecular Biology


    Dive into the research topics of 'Identification of a second DNA binding site in the human Rad52 protein'. Together they form a unique fingerprint.

    Cite this