Koterov A N, Novoradovskaia N A, Filippovich I V
Biokhimiia. 1988 Aug;53(8):1278-87.
The effect of a single-stranded DNA-binding protein (SSB-protein) form Ehrlich ascites tumour cells (EAT) on the activity of homologous purified DNA-polymerases alpha and beta, DNA-replicase, primase and DNA-polymerases from phage T4 and Bacillus stearothermophillus was studied. It was shown that the SSB-protein caused a 1.5-2.5-fold stimulation of the DNA-polymerase alpha activity on different templates (e.g., denaturated and activated DNA, poly(dA). The degree of stimulation depended on the template type, protein/template ratio and purity of DNA-polymerase alpha. The activity of DNA-polymerase was inhibited by the SSB-protein, when the activated DNA was used as a matrix and was unchanged on the denaturated DNA. The activity of some prokaryotic DNA-polymerases was increased under the influence of the SSB-protein. The protein enhanced the processivity of T4 DNA-polymerase and strongly inhibited the activity of replicase and primase. A conclusion about the complex effect of the SSB-protein on the activity of replicative and repair enzymes is drawn.
研究了来自艾氏腹水瘤细胞(EAT)的单链DNA结合蛋白(SSB蛋白)对同源纯化的DNA聚合酶α和β、DNA复制酶、引发酶以及噬菌体T4和嗜热脂肪芽孢杆菌的DNA聚合酶活性的影响。结果表明,SSB蛋白在不同模板(如变性和活化的DNA、聚(dA))上可使DNA聚合酶α的活性提高1.5至2.5倍。刺激程度取决于模板类型、蛋白质/模板比例以及DNA聚合酶α的纯度。当以活化的DNA作为基质时,DNA聚合酶的活性受到SSB蛋白的抑制,而在变性DNA上则保持不变。在SSB蛋白的影响下,一些原核DNA聚合酶的活性有所增加。该蛋白增强了T4 DNA聚合酶的持续合成能力,并强烈抑制了复制酶和引发酶的活性。得出了关于SSB蛋白对复制和修复酶活性具有复杂影响的结论。