Stürzbecher H W, Chumakov P, Welch W J, Jenkins J R
Marie Curie Research Institute, The Chart, Oxted, Surrey, UK.
Oncogene. 1987 May;1(2):201-11.
We have examined the expression of a series of mouse mutant, as well as wild-type, p53 proteins in SV40-transformed monkey COS cells. Wild-type mouse p53 binds predominantly to SV40 large T antigen in these cells. However, several of the mutants co-precipitate exclusively with proteins of approximately 68 Kd relative molecular mass. We show by immunological and proteolytic mapping techniques that these proteins are identical to the hsp 72/73 heat shock proteins. p53 mutants in complex with hsp 72/73 have an altered subcellular location compared to the wild-type protein and the hsp 72/73 binding p53 mutants fail to exhibit an epitope recognized by monoclonal antibody PAb 246. The existence of at least two antigenically distinct subclasses of hsp 72/73 complexed to mutant p53 is shown.
我们检测了一系列小鼠突变型以及野生型p53蛋白在SV40转化的猴COS细胞中的表达情况。在这些细胞中，野生型小鼠p53主要与SV40大T抗原结合。然而，有几个突变体仅与相对分子质量约为68 Kd的蛋白质共沉淀。我们通过免疫和蛋白水解图谱技术表明，这些蛋白质与hsp 72/73热休克蛋白相同。与野生型蛋白相比，与hsp 72/73形成复合物的p53突变体具有改变的亚细胞定位，并且与hsp 72/73结合的p53突变体未能表现出单克隆抗体PAb 246识别的表位。结果显示，至少存在两种与突变型p53复合的抗原性不同的hsp 72/73亚类。
