The in vitro activity of a Rad55 homologue from Sulfolobus tokodaii, a candidate mediator in RadA-catalyzed homologous recombination
The in vitro activity of a Rad55 homologue from Sulfolobus tokodaii, a candidate mediator in RadA-catalyzed homologous recombination
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来自 Sulfolobus tokodaii 的 Rad55 同源物（RadA 催化同源重组的候选介体）的体外活性
DOI：
10.1007/s00792-007-0113-y
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发表时间：
2008-01-01
期刊：
影响因子：
2.9
通讯作者：
Shen, Yulong
中科院分区：
文献类型：
--
作者：
Sheng, Duohong;Zhu, Shanshan;Shen, Yulong
类胡萝卜素具有与真核生物相似的重组蛋白，但许多尚未被鉴定。在这里，Rad55同源物从硫化叶菌tokodaii（stRad55A）的特性进行了报道。StRad55A蛋白优先与ssDNA结合，具有ssDNA依赖的ATP酶活性。此外，紫外光也能诱导该蛋白的表达，这与广古菌中的RadA蛋白RadB不同。最重要的是，stRad55A可以释放过量的stSSB（来自S. tokodaii）对stRadA（来自S. tokodaii），通过直接与stRadA和stSSB相互作用。StRad55A可能作为介导剂加速stRadA对stSSB的置换。
Archaea have recombination proteins similar to those of eukaryote, but many have not been characterized. Here, the characterization of a Rad55 homologue from Sulfolobus tokodaii (stRad55A) was reported. StRad55A protein preferred binding to ssDNA and had ssDNA-dependent ATPase activity. In addition, UV light could induce the expression of this protein, which was different from RadB, a RadA paralog found in euryarchaeota. Most importantly, stRad55A could release the suppression of excessive stSSB (single strand DNA binding protein from S. tokodaii) on the strand exchange catalyzed by stRadA (RadA homologue from S. tokodaii), by interacting directly with both stRadA and stSSB. StRad55A may function as a mediator to accelerate the displacement of stSSB by stRadA.