Structure and subunit composition of the RuvAB-Holliday junction complex.
Structure and subunit composition of the RuvAB-Holliday junction complex.
复制标题
DOI：
10.1006/jmbi.1996.0799
复制
发表时间：
1997-02
影响因子：
5.6
通讯作者：
X. Yu;S. C. West;E. Egelman
中科院分区：
文献类型：
--
作者：
X. Yu;S. C. West;E. Egelman
急诊大肠杆菌RuvA和RuvB蛋白参与重组的晚期和受损DNA的重组修复，与Holliday连接结合并促进分支迁移。我们已经使用电子显微镜和图像分析来检查RuvA和RuvB绑定到模型霍利迪结构。RuvB的两个六聚体环以双极方式取向，使得每个六聚体环的大端面向接合处。结果表明，分支迁移的模型，其中DNA被泵出的小端的每个环作为ATP被水解。相同的结构极性已经建立了噬菌体T7 gp4复制解旋酶。质量和图像分析的RuvAB连接复合物表明，两个四聚体的RuvA形成一个对称的三明治平面的交界处。
The E. coli RuvA and RuvB proteins, which are involved in the late stages of recombination and the recombinational repair of damaged DNA, bind to Holliday junctions and promote branch migration. We have used electron microscopy and image analysis to examine RuvA and RuvB bound to model Holliday structures. The two hexameric rings of RuvB are oriented in a bipolar manner, so that the large end of each faces the junction. The results suggest a model for branch migration in which DNA is pumped out of the small end of each ring as ATP is hydrolyzed. The same structural polarity has been established for the bacteriophage T7 gp4 replicative helicase. Mass and image analysis of the RuvAB-junction complex suggests that two tetramers of RuvA form a symmetrical sandwich about the plane of the junction.