ATP-dependent DNA binding, unwinding, and resection by the Mre11/Rad50…
[2015 EMBO] ATP-dependent DNA binding, unwinding, and resection by the Mre11Rad50 complex.pdf - 담당교수Yunje Cho
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- 작성자최고관리자
- 2017-09-28
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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 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
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
