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首页> 外文期刊>Biochemistry >Mycobacterium tuberculosis RuvA Induces Two Distinct Types of Structural Distortions between the Homologous and Heterologous Holliday Junctions
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Mycobacterium tuberculosis RuvA Induces Two Distinct Types of Structural Distortions between the Homologous and Heterologous Holliday Junctions

机译：结核分枝杆菌RuvA诱导同源和异源霍利迪结之间的两种不同类型的结构畸变

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摘要

A central step in the process of homologous genetic recombination is the strand exchange between two homologous DNA molecules, leading to the formation of the Holliday junction intermediate. Several lines of evidence, both in vitro and in vivo, suggest a concerted role for the Escherichia coli RuvABC protein complex in the process of branch migration and the resolution of the Holliday junctions. A number of investigations have examined the role of RuvA protein in branch migration of the Holliday junction in conjunction with its natural cellular partner, RuvB. However, it remains unclear whether the RuvABC protein complex or its individual subunits function differently in the context of DNA repair and homologous recombination. In this study, we have specifically investigated the function of RuvA protein using Holliday junctions containing either homologous or heterologous arms. Our data show that Mycobacterium tuberculosis ruvA complements E. coli ΔruvA mutants for survival to genotoxic stress caused by different DNA-damaging agents, and the purified RuvA protein binds HJ in preference to any other substrates. Strikingly, our analysis revealed two distinct types of structural distortions caused by M. tuberculosis RuvA between the homologous and heterologous Holliday junctions. We interpret these data as evidence that local distortion of base pairing in the arms of homologous Holliday junctions by RuvA might augment branch migration catalyzed by RuvB. The biological significance of two modes of structural distortion caused by M. tuberculosis RuvA and the implications for its role in DNA repair and homologous recombination are discussed.
机译：同源基因重组过程中的中心步骤是两个同源DNA分子之间的链交换，从而导致形成霍利迪连接中间体。体外和体内的一些证据表明，大肠杆菌RuvABC蛋白复合物在分支迁移和霍利迪连接的解析中起着协同作用。大量研究已经研究了RuvA蛋白及其天然细胞伴侣RuvB在霍利迪交界处分支迁移中的作用。然而，目前尚不清楚RuvABC蛋白复合物或其单个亚基在DNA修复和同源重组中的功能是否不同。在这项研究中，我们使用含有同源或异源臂的霍利迪连接点专门研究了RuvA蛋白的功能。我们的数据表明，结核分枝杆菌ruvA可以补充大肠杆菌ΔruvA突变体，以抵抗由不同的DNA破坏剂引起的基因毒性胁迫，并且纯化的RuvA蛋白优先结合HJ与任何其他底物。令人惊讶的是，我们的分析揭示了同源和异源霍利迪结点之间结核分枝杆菌RuvA引起的两种不同类型的结构变形。我们将这些数据解释为证据，证明RuvA在同源霍利迪交界处的臂部碱基配对的局部变形可能会增强RuvB催化的分支迁移。讨论了结核分枝杆菌RuvA引起的两种结构变形模式的生物学意义及其在DNA修复和同源重组中的作用。

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