Structure of the human DNA-repair protein RAD52 containing surface mutations

Mika Saotome, Kengo Saito, Keiichi Onodera, Hitoshi Kurumizaka, Wataru Kagawa*

*Corresponding author for this work

    Research output: Contribution to journalArticlepeer-review

    2 Citations (Scopus)


    The Rad52 protein is a eukaryotic single-strand DNA-annealing protein that is involved in the homologous recombinational repair of DNA double-strand breaks. The isolated N-terminal half of the human RAD52 protein (RAD521-212) forms an undecameric ring structure with a surface that is mostly positively charged. In the present study, it was found that RAD521-212 containing alanine mutations of the charged surface residues (Lys102, Lys133 and Glu202) is highly amenable to crystallization. The structure of the mutant RAD521-212 was solved at 2.4 Å resolution. The structure revealed an association between the symmetry-related RAD521-212 rings, in which a partially unfolded, C-terminal region of RAD52 extended into the DNA-binding groove of the neighbouring ring in the crystal. The alanine mutations probably reduced the surface entropy of the RAD521-212 ring and stabilized the ring-ring association observed in the crystal.

    Original languageEnglish
    Pages (from-to)598-603
    Number of pages6
    JournalActa Crystallographica Section F:Structural Biology Communications
    Publication statusPublished - 2016


    • higher order interaction
    • homologous recombinational repair
    • RAD52
    • single-strand annealing proteins
    • ssDNA-binding protein
    • surface-entropy reduction

    ASJC Scopus subject areas

    • Structural Biology
    • Biophysics
    • Biochemistry
    • Genetics
    • Condensed Matter Physics


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