ATP-dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex > 연구성과

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ATP-dependent DNA binding, unwinding, and resection by the Mre11/Rad50…

  • 저널명The EMBO Journal (2016) Apr 1;35(7):743-58
    • 담당교수[2016년 04월] 조윤제 교수연구실
    • 조회932
    • 작성자최고관리자
    • 2017-09-28



    ATP-dependent DNA end recognition and nucleolytic processing are central functions of the Mre11/Rad50 (MR) complex in DNA
    double-strand break repair. However, it is still unclear how ATP binding and hydrolysis primes the MR function and regulates
    repair pathway choice in cells. Here, Methanococcus jannaschii MRATPcS-DNA structure reveals that the partly deformed DNA runs symmetrically across central groove between two ATPcS-bound Rad50 nucleotide-binding domains. Duplex DNA cannot access the Mre11 active site in the ATP-free full-length MR complex. ATP hydrolysis drives rotation of the nucleotide-binding domain and
    induces the DNA melting so that the substrate DNA can access Mre11. Our findings suggest that the ATP hydrolysis-driven conformational changes in both DNA and the MR complex coordinate the melting and endonuclease activity

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