ATP-dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex
SCIE
SCOPUS
- Title
- ATP-dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex
- Authors
- Liu, Y; Sung, S; Kim, Y; Li, FY; Gwon, G; Jo, A; Kim, AK; Kim, T; Song, OK; Lee, SE; Cho, Y
- Date Issued
- 2016-04-01
- Publisher
- Nature Publishing Group
- Abstract
- 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-ATP gamma S-DNA structure reveals that the partly deformed DNA runs symmetrically across central groove between two ATP gamma S-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.
- URI
- https://oasis.postech.ac.kr/handle/2014.oak/36742
- DOI
- 10.15252/embj.201592462
- ISSN
- 0261-4189
- Article Type
- Article
- Citation
- EMBO Journal, vol. 35, no. 7, page. 743 - 758, 2016-04-01
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