RUVC PROTEIN RESOLVES HOLLIDAY JUNCTIONS VIA CLEAVAGE OF THE CONTINUOUS (NONCROSSOVER) STRANDS
RUVC PROTEIN RESOLVES HOLLIDAY JUNCTIONS VIA CLEAVAGE OF THE CONTINUOUS (NONCROSSOVER) STRANDS
复制标题
DOI：
10.1073/pnas.92.12.5635
复制
发表时间：
1995-06-06
影响因子：
11.1
通讯作者：
WEST, SC
中科院分区：
文献类型：
--
作者：
BENNETT, RJ;WEST, SC
大肠杆菌的 RuvC 蛋白在基因重组和 DNA 损伤的复制后修复过程中解析霍利迪连接体。使用受限于采用定义的异构体构型的合成霍利迪连接体，我们表明通过对称切割连续（非交叉）DNA 链对来实现解析。该结果与用噬菌体 T4 核酸内切酶 VII 观察到的结果形成对比，后者切割一对交叉链。在存在 RuvC 的情况下，这对连续链（即裂解的目标链）表现出对羟基自由基的超敏性。这些结果表明，连续链在 RuvC/Holliday 连接复合物内发生扭曲，并且 RuvC 介导的解析事件需要对四向连接进行蛋白质指导的结构变化。
The RuvC protein of Escherichia coli resolves Holliday junctions during genetic recombination and the postreplicational repair of DNA damage, Using synthetic Holliday junctions that are constrained to adopt defined isomeric configurations, we show that resolution occurs by symmetric cleavage of the continuous (noncrossing) pair of DNA strands. This result contrasts with that observed with phage T4 endonuclease VII, which cleaves the pair of crossing strands. In the presence of RuvC, the pair of continuous strands (i.e., the target strands for cleavage) exhibit a hypersensitivity to hydroxyl radicals, These results indicate that the continuous strands are distorted within the RuvC/Holliday junction complex and that RuvC-mediated resolution events require protein-directed structural changes to the four-way junction.