Structural highlights
Function
MRE11_METJA Involved in DNA double-strand break repair (DSBR). The Rad50/Mre11 complex possesses single-strand endonuclease activity and ATP-dependent double-strand-specific 3'-5' exonuclease activity (By similarity).
Publication Abstract from PubMed
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-ATPgammaS-DNA structure reveals that the partly deformed DNA runs symmetrically across central groove between two ATPgammaS-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 binding, unwinding, and resection by the Mre11/Rad50 complex.,Liu Y, Sung S, Kim Y, Li F, Gwon G, Jo A, Kim AK, Kim T, Song OK, Lee SE, Cho Y EMBO J. 2015 Dec 30. pii: e201592462. PMID:26717941[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Liu Y, Sung S, Kim Y, Li F, Gwon G, Jo A, Kim AK, Kim T, Song OK, Lee SE, Cho Y. ATP-dependent DNA binding, unwinding, and resection by the Mre11/Rad50 complex. EMBO J. 2015 Dec 30. pii: e201592462. PMID:26717941 doi:http://dx.doi.org/10.15252/embj.201592462
