A unique β-hairpin protruding from AAA+ ATPase domain of RuvB motor protein is involved in the interaction with RuvA DNA recognition protein for branch migration of Holliday junctions
A unique β-hairpin protruding from AAA+ ATPase domain of RuvB motor protein is involved in the interaction with RuvA DNA recognition protein for branch migration of Holliday junctions
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DOI：
10.1074/jbc.m103611200
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发表时间：
2001-09-14
影响因子：
4.8
通讯作者：
Shinagawa, H
中科院分区：
文献类型：
--
作者：
Han, YW;Iwasaki, H;Shinagawa, H
大肠杆菌RuvB蛋白是与RuvA形成复合物并在同源重组期间促进霍利迪连接的分支迁移的马达蛋白。本研究描述了两种RuvB突变体I148 T和I150 T的特征，它们在RuvA存在下不促进分支迁移。这些RuvB突变体水解ATP和结合双链体DNA的效率与野生型RuvB相同，但突变体不与RuvA形成复合物，并且在RuvA辅助的方式下装载到连接DNA上有缺陷。最近的晶体学研究显示Ile（148）和Ile（150）处于从RuvB的AAA（+）ATP酶结构域突出的独特β-发夹中。我们提出，这种β-发夹与RuvA的移动的第三结构域中的疏水残基相互作用，并且这种相互作用对于RuvA辅助的RuvB加载到Holliday连接DNA上至关重要。
The Escherichia coh RuvB protein is a motor protein that forms a complex with RuvA and promotes branch migration of Holliday junctions during homologous recombination. This study describes the characteristics of two RuvB mutants, I148T and I150T, that do not promote branch migration in the presence of RuvA. These RuvB mutants hydrolyzed ATP and bound duplex DNA with the same efficiency as wild-type RuvB, but the mutants did not form a complex with RuvA and were defective in loading onto junction DNA in a RuvA-assisted manner. A recent crystallographic study revealed that Ile(148) and Ile(150) are in a unique beta -hairpin that protrudes from the AAA(+) ATPase domain of RuvB. We propose that this beta -hairpin interacts with hydrophobic residues in the mobile third domain of RuvA and that this interaction is vital for the RuvA-assisted loading of RuvB onto Holliday junction DNA.