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

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-ATPS-DNA structure reveals that the partly deformed DNA runs symmetrically across central groove between two ATPS-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.
Source: EMBO Journal - Category: Molecular Biology Authors: Tags: DNA Replication, Repair & Recombination, Structural Biology Articles Source Type: research

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Source: Revista Brasileira de Cirurgia Cardiovascular - Category: Cardiovascular & Thoracic Surgery Source Type: research
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Source: Journal of Clinical Investigation - Category: Biomedical Science Authors: Source Type: research
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Source: ABC News: Health - Category: Consumer Health News Tags: Health Source Type: news
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Source: GEO: Gene Expression Omnibus - Category: Genetics & Stem Cells Tags: Expression profiling by high throughput sequencing Homo sapiens Source Type: research
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