Yamada Kazuhiro, Ariyoshi Mariko, Morikawa Kosuke
Biomolecular Engineering Research Institute, 6-2-3 Furuedai, Suita, Osaka 565-0874, Japan.
Curr Opin Struct Biol. 2004 Apr;14(2):130-7. doi: 10.1016/j.sbi.2004.03.005.
The processing of the Holliday junction by various proteins is a major event in DNA homologous recombination and is crucial to the maintenance of genome stability and biological diversity. The proteins RuvA, RuvB and RuvC play central roles in the late stage of recombination in prokaryotes. Recent atomic views of these proteins, including protein-protein and protein-junction DNA complexes, provide new insights into branch migration mechanisms: RuvA is likely to be responsible for base-pair rearrangements, whereas RuvB, classified as a member of the AAA(+) family, functions as a pump to pull DNA duplex arms without segmental unwinding. The mechanism of junction resolution by RuvC in the RuvABC resolvasome remains to be elucidated.
多种蛋白质对霍利迪连接体的加工是DNA同源重组中的一个重大事件,对维持基因组稳定性和生物多样性至关重要。蛋白质RuvA、RuvB和RuvC在原核生物重组后期发挥核心作用。这些蛋白质的最新原子结构视图,包括蛋白质-蛋白质和蛋白质-连接体DNA复合物,为分支迁移机制提供了新的见解:RuvA可能负责碱基对重排,而被归类为AAA(+)家族成员的RuvB则起到泵的作用,拉动DNA双链臂而不进行片段解旋。RuvABC解离体中RuvC进行连接体拆分的机制仍有待阐明。