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

机译:ATP-dependent DNA结合,解除切除Mre11 / Rad50复杂

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摘要

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.
机译:ATP-dependent DNA识别和nucleolytic结束加工中心的功能Mre11 / Rad50 (MR)复杂的DNA双链打破修复。ATP绑定和水解质数先生函数在细胞和调节修复途径的选择。在这里,产甲烷球菌属jannaschii MR-ATP伽马dnaDNA结构显示,部分变形中部槽之间的对称运行两个ATP伽马S-bound Rad50 nucleotide-binding域。活跃的站点ATP-free全身复杂。nucleotide-binding域和诱发的DNA融化的衬底DNA可以访问Mre11。hydrolysis-driven构象的变化DNA和复杂的协调融化和先生核酸内切酶的活动。

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