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

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


    研究成果: Article査読

    2 被引用数 (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.

    ジャーナルActa Crystallographica Section F:Structural Biology Communications
    出版ステータスPublished - 2016

    ASJC Scopus subject areas

    • 構造生物学
    • 生物理学
    • 生化学
    • 遺伝学
    • 凝縮系物理学


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