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

Yaqi Liu, Sihyun Sung, Youngran Kim, Fuyang Li, Gwanghyun Gwon, Aera Jo, Ae Kyoung Kim, Taeyoon Kim, Ok kyu Song, Sang Lee, Yunje Cho

Research output: Contribution to journalArticle

45 Scopus citations


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 MR-ATPγS-DNA structure reveals that the partly deformed DNA runs symmetrically across central groove between two ATPγS-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.

Original languageEnglish (US)
JournalEMBO Journal
StateAccepted/In press - 2015


  • Central groove
  • DNA binding
  • DNA melting
  • Mre11/Rad50
  • Nuclease

ASJC Scopus subject areas

  • Molecular Biology
  • Biochemistry, Genetics and Molecular Biology(all)
  • Immunology and Microbiology(all)
  • Neuroscience(all)

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    Liu, Y., Sung, S., Kim, Y., Li, F., Gwon, G., Jo, A., Kim, A. K., Kim, T., Song, O. K., Lee, S., & Cho, Y. (Accepted/In press). ATP-dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex. EMBO Journal.