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首页> 外文期刊>Molecular cell >Substrate Specificity of RusA Resolvase Reveals the DNA Structures Targeted by RuvAB and RecG In Vivo
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Substrate Specificity of RusA Resolvase Reveals the DNA Structures Targeted by RuvAB and RecG In Vivo

机译：RusA溶解酶的底物特异性揭示了RuvAB和RecG体内靶向的DNA结构

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摘要

RusA endonuclease cleaves Holliday junctions by introducing paired strand incisions 5' to CC dinucleotides. Coordinated catalysis is achieved when both subunits of the homodimer interact simultaneously with cleavage sites located symmetrically. This requirement confers Holliday junction specificity. Uncoupled catalysis occurs when binding interactions are disturbed. Genetic studies indicate that uncoupling occurs rarely in vivo, and DNA cleavage is therefore restricted to Holliday junctions. We exploited the specificity of RusA to identify the DNA substrates targeted by the RuvAB and RecG branch-migration proteins in vivo. We present evidence that replication restart in UV-irradiated cells relies on the processing of stalled replication forks by RecG helicase and of Holliday junctions by the RuvABC resolvasome, and that RuvAB alone may not promote repair.
机译：RusA核酸内切酶通过将配对链切口5'引入CC二核苷酸来切割霍利迪连接。当同型二聚体的两个亚基与对称定位的切割位点同时相互作用时，可实现催化催化。该要求赋予霍利迪连接特异性。当结合相互作用被干扰时，发生非偶联催化。遗传研究表明，解偶联很少在体内发生，因此DNA切割仅限于霍利迪连接。我们利用RusA的特异性来鉴定RuvAB和RecG分支迁移蛋白在体内靶向的DNA底物。我们目前的证据表明，在紫外线照射的细胞中，复制重启依赖于由RecG解旋酶处理停止的复制叉和由RuvABC Resolvasome处理的Holliday连接，并且单独的RuvAB可能不会促进修复。

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