Altered DNA binding by the human Rad51-R150Q mutant found in breast cancer patients

Takako Ishida, Yoshimasa Takizawa, Isao Sakane, Hitoshi Kurumizaka*

*この研究の対応する著者

    研究成果: Article査読

    12 被引用数 (Scopus)

    抄録

    The human Rad51 protein (HsRad51) catalyzes homologous pairing and strand exchange between single-stranded DNA (ssDNA) and double-stranded DNA (dsDNA) during recombinational repair of double-stranded DNA breaks. An HsRad51 mutation that results in the substitution of Gln for Arg150 (R150Q) was found in bilateral breast cancer patients; however, the consequences of this R150Q mutation have not been elucidated. To determine how this HsRad51(R150Q) mutation affects HsRad51 function, in the present study, we purified the HsRad51(R150Q) mutant. The purified HsRad51(R150Q) was completely proficient in the ATP-hydrolyzing activity. A gel filtration analysis revealed that HsRad51(R150Q) also retained the polymer formation ability. In contrast, the ssDNA- and dsDNA-binding abilities of HsRad51(R150Q) were clearly reduced, as compared to those of HsRad51. These differences in the DNA-binding properties between HsRad51(R150Q) and HsRad51 may be important to account for the tumorigenesis in breast cancer patients with the HsRad51(R150Q) mutation.

    本文言語English
    ページ(範囲)1374-1378
    ページ数5
    ジャーナルBiological and Pharmaceutical Bulletin
    30
    8
    DOI
    出版ステータスPublished - 2007 8月

    ASJC Scopus subject areas

    • 分子医療
    • 薬理学、毒性学および薬学(全般)

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