STIMULATION OF T7 DNA-POLYMERASE BY A NEW PHAGE-CODED PROTEIN
STIMULATION OF T7 DNA-POLYMERASE BY A NEW PHAGE-CODED PROTEIN
复制标题
DOI：
10.1007/bf00271243
复制
发表时间：
1973-01-01
期刊：
影响因子：
--
通讯作者：
JOST, E
中科院分区：
文献类型：
--
作者：
SCHERZINGER, E;LITFIN, F;JOST, E
从 T7 感染的大肠杆菌中纯化出噬菌体诱导的 DNA 结合蛋白。大肠杆菌。经SDS-聚丙烯酰胺凝胶电泳判断，该蛋白分子量约为25000。纯化的蛋白质与单链结合，但不与天然 T7 DNA 结合。就像大肠杆菌的 T4 基因 32 蛋白和 22000 道尔顿“解旋蛋白”一样。在大肠杆菌中，T7 25000 蛋白可降低聚 d(A-T) 的熔解温度。该蛋白使用部分单链 T7 DNA 作为模板引物，可将 T7 DNA 聚合酶的体外 DNA 合成刺激约五倍。还发现大肠杆菌的DNA解旋蛋白。大肠杆菌对 T7 DNA 聚合酶的刺激程度大致相同。然而，这两种解旋蛋白均不会刺激 DNA 聚合酶 I of E。大肠杆菌。
A bacteriophage-induced DNA-binding protein was purified from T7 infectedE. coli. The protein has a molecular weight of about 25000, as judged by SDS-polyacrylamide gel electrophoresis. The purified protein binds to single-stranded but not to native T7 DNA. Like the T4 gene-32 protein and the 22000-dalton “unwinding protein” ofE. coli, the T7 25000 protein lowers the melting temperature of poly d(A-T). Using partially single-stranded T7 DNA as template-primer, the protein stimulatesin vitroDNA synthesis by T7 DNA polymerase about five-fold. It was also found that the DNA-unwinding protein ofE. colistimulates T7 DNA polymerase to approximately the same extent. However, neither of the unwinding proteins stimulate DNA polymerase I ofE. coli.