Jenkins J R, Chumakov P, Addison C, Stürzbecher H W, Wade-Evans A
Cell Proliferation Laboratory, Marie Curie Research Institute, Oxted, Surrey, England.
J Virol. 1988 Oct;62(10):3903-6. doi: 10.1128/JVI.62.10.3903-3906.1988.
We mapped regions of the mouse p53 primary amino acid sequence implicated in stable complex formation with simian virus 40 T antigen. A number of mutant p53 proteins failed to complex stably with T antigen in vivo but formed stable complexes with T antigen in in vitro association assays. In contrast to an earlier report (T.-H. Tan, H. Wallis, and A. J. Levine, J. Virol. 59:574-583, 1986), our study showed that two distinct regions of p53 primary amino acid sequence, highly conserved between mouse and Xenopus laevis, were implicated in stable complex formation. Our data support the proposal that, when in complex, T antigen may occupy a site on p53 that is implicated in the normal function of the protein.
我们绘制了小鼠p53主要氨基酸序列中与猿猴病毒40 T抗原形成稳定复合物相关的区域。许多突变型p53蛋白在体内不能与T抗原稳定结合，但在体外结合试验中能与T抗原形成稳定复合物。与早期的一份报告（T.-H. Tan、H. Wallis和A. J. Levine，《病毒学杂志》59:574 - 583，1986年）相反，我们的研究表明，p53主要氨基酸序列中有两个不同区域在小鼠和非洲爪蟾之间高度保守，它们与稳定复合物的形成有关。我们的数据支持这样一种观点，即当形成复合物时，T抗原可能占据p53上一个与该蛋白正常功能相关的位点。
