Characterization of mutant p53-hsp72/73 protein-protein complexes by transient expression in monkey COS cells.
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.
Stürzbecher
H W
HW
Cell Proliferation Laboratory, Marie Curie Research Institute, Oxted, Surrey, England.
Addison
C
C
Jenkins
J R
JR
D000818:Animals; D002460:Cell Line; D002471:Cell Transformation, Neoplastic; D002872:Chromosome Deletion; D004251:DNA Transposable Elements; D005796:Genes; D006360:Heat-Shock Proteins / Q000235:genetics* / Q000378:metabolism; D009154:Mutation; D009363:Neoplasm Proteins / Q000235:genetics* / Q000378:metabolism; D009687:Nuclear Proteins / Q000235:genetics*; D010750:Phosphoproteins / Q000235:genetics* / Q000378:metabolism; D010957:Plasmids; D014176:Protein Biosynthesis; D013539:Simian virus 40 / Q000235:genetics; D014158:Transcription, Genetic; D016159:Tumor Suppressor Protein p53
D004251:DNA Transposable Elements; D006360:Heat-Shock Proteins; D009363:Neoplasm Proteins; D009687:Nuclear Proteins; D010750:Phosphoproteins; D016159:Tumor Suppressor Protein p53