DNA polymerase V and RecA protein, a minimal mutasome.
DNA polymerase V and RecA protein, a minimal mutasome.
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DNA 聚合酶 V 和 RecA 蛋白（一种最小突变体）。
DOI：
10.1016/j.molcel.2005.01.006
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发表时间：
2005
期刊：
影响因子：
16
通讯作者：
Goodman,MyronF
中科院分区：
文献类型：
--
作者：
Schlacher,Katharina;Leslie,Kris;Wyman,Claire;Woodgate,Roger;Cox,MichaelM;Goodman,MyronF
大肠杆菌SOS反应的一个标志是由跨损伤合成（TLS）引起的突变大量增加。TLS需要DNA聚合酶V（UmuD′2C）和RecA。在这里，我们表明，pol V和RecA相互作用的两种不同的机制。首先，pol V在没有DNA和ATP的情况下与RecA结合，其次，通过其UmuD′亚基，需要DNA和ATP而不需要ATP水解。TLS在没有RecA核蛋白丝的情况下发生，但在其存在下被抑制。因此，RecA核蛋白丝不太可能是SOS诱变所需的。Pol V活性在不存在RecA或存在RecA1730的情况下严重降低，RecA1730是体内Pol V诱变缺陷的突变体。Pol V活性强烈增强与RecA突变体组成的诱变在体内，这表明RecA是一个专性的辅助因子，激活pol V SOS诱变。
A hallmark of theEscherichia coliSOS response is the large increase in mutations caused by translesion synthesis (TLS). TLS requires DNA polymerase V (UmuD′2C) and RecA. Here, we show that pol V and RecA interact by two distinct mechanisms. First, pol V binds to RecA in the absence of DNA and ATP and second, through its UmuD′ subunit, requiring DNA and ATP without ATP hydrolysis. TLS occurs in the absence of a RecA nucleoprotein filament but is inhibited in its presence. Therefore, a RecA nucleoprotein filament is unlikely to be required for SOS mutagenesis. Pol V activity is severely diminished in the absence of RecA or in the presence of RecA1730, a mutant defective for pol V mutagenesis in vivo. Pol V activity is strongly enhanced with RecA mutants constitutive for mutagenesis in vivo, suggesting that RecA is an obligate accessory factor that activates pol V for SOS mutagenesis.