Stürzbecher H W, Addison C, Jenkins J R
Cell Proliferation Laboratory, Marie Curie Research Institute, Oxted, Surrey, England.
Mol Cell Biol. 1988 Sep;8(9):3740-7. doi: 10.1128/mcb.8.9.3740-3747.1988.
Several mutant, but not wild-type, p53 proteins form complexes with hsp72/73 heat shock-related proteins in simian virus 40-transformed monkey COS cells. We carried out a detailed biochemical and structural mapping analysis of p53 and report here that p53-hsp72/73 complex formation showed considerable structural specificity. Such complexes were remarkably stable, but unlike analogous complexes formed between p53 and simian virus 40 T antigen, they did not form in in vitro association assays. p53-hsp72/73 complex formation in vivo appears to be dependent on aspects of mutant p53 protein conformation. However, absence of the conformation-sensitive epitope recognized by monoclonal antibody PAb 246 was not reliably diagnostic of such complexes, nor was p53-hsp72173 binding reliably diagnostic of oncogenic activation.
在猿猴病毒40转化的猴COS细胞中，几种突变型而非野生型p53蛋白与hsp72/73热休克相关蛋白形成复合物。我们对p53进行了详细的生化和结构图谱分析，并在此报告p53与hsp72/73复合物的形成显示出相当大的结构特异性。此类复合物非常稳定，但与p53和猿猴病毒40 T抗原之间形成的类似复合物不同，它们在体外结合试验中并未形成。体内p53与hsp72/73复合物的形成似乎取决于突变型p53蛋白构象的某些方面。然而，单克隆抗体PAb 246识别的构象敏感表位的缺失并不能可靠地诊断此类复合物，p53与hsp72/73的结合也不能可靠地诊断致癌激活。
