p53 and DNA polymerase α compete for binding to SV40 T antigen
p53 and DNA polymerase α compete for binding to SV40 T antigen
复制标题
p53 和 DNA 聚合酶 α 竞争与 SV40 T 抗原的结合
作者：
Julian Gannon;David P. Lane
猴病毒40的大T抗原(T)是病毒DNA复制和细胞转化所必需的多功能蛋白1。在病毒感染和转化的细胞中，T抗原与宿主蛋白p53形成特异性蛋白复合物2 - 4。P53最近被证明是致癌基因5 - 7，但其正常功能尚不清楚。我们之前建立了一种放射免疫-免疫测定法8来研究新描述的T抗原和DNA聚合酶α之间的复合物，并注意到p53和聚合酶结合在T中诱导的抗原变化之间的相似性9,10。我们现在将这一分析扩展到更大的抗T抗体集合，并正式确定p53和DNA聚合酶α可以竞争与SV40 T抗原的结合。在这三种成分的临界浓度下，可以检测到T、p53和DNA聚合酶α的三聚体复合物。我们的观察结果对这些核癌基因在正常和转化细胞中控制病毒和细胞DNA合成以及病毒宿主范围具有重要意义。我们提出了p53在生长控制中的作用模型。
The large T antigen (T) of simian virus 40 is a multifunctional protein required for both viral DNA replication and cellular transformation1. T antigen forms specific protein complexes with the host protein p53 in both virus-infected and transformed cells2–4. p53 has recently been shown to be an oncogene5–7, but its normal function is not clear. We previously established a radioim-munoassay8 to study the newly described complex between T antigen and DNA polymerase α, and have noted a similarity between the antigenic changes induced in T by the binding of both p53 and polymerase9,10. We now extend this analysis to a larger collection of anti-T antibodies and formally establish that p53 and DNA polymerase α can compete for binding to the SV40 T antigen. At a critical concentration of the three components it is possible to detect a trimeric complex of T, p53 and DNA polymerase α. Our observations have important implications for the control by these nuclear oncogenes of viral and cellular DNA synthesis and viral host range in both normal and transformed cells. We present a model for the action of p53 in growth control.
抗人DNA聚合酶α单克隆抗体的制备和初步表征。
DOI：
--
发表时间：
1982
期刊：
The Journal of biological chemistry
影响因子：
--
作者：
Tanaka,S;Hu,SZ;Wang,TS;Korn,D
通讯作者：
Korn,D