Wild-type and mutant p53 proteins exhibit opposing activities in respectively suppressing and promoting tumour development. In a rat embryo fibroblast cell line transformed with a murine temperature-sensitive p53 gene, p53 functions as a oncogene at 37 degrees C and as a tumour suppressor at 32 degrees C [Michalovitz, D., Halevy, O. & Oren, M. (1990). Cell, 62, 671-680]. We have used this cell line to investigate whether this temperature-dependent switching of function involves changes in the phosphorylation of p53 protein. Monoclonal antibodies PAb246 and PAb240 were used to immunoprecipitate metabolically 32P-labelled p53 protein in the 'wild-type' or mutant conformation from cells grown at 32 degrees C or 37 degrees C. Tryptic phosphopeptide maps were prepared from the isolated 'wild-type' and mutant p53 proteins. At 32 degrees C and 37 degrees C phosphopeptide maps of the 'wild-type' and mutant protein were identical. This demonstrates that the temperature-dependent conformation change, and associated functional change, in the p53 protein does not involve a change in the state of phosphorylation.
|Number of pages||3|
|Publication status||Published - Aug 1992|
Picksley, S. M., Meek, D. W., & Lane, D. P. (1992). The conformational change of a murine temperature-sensitive p53 protein is independent of a change in phosphorylation status. Oncogene, 7(8), 1649-1651. http://www.scopus.com/results/results.url?sort=plf-f&src=s&st1=The+conformational+change+of+a+murine+temperature-sensitive+p53+protein+is+independent+of+a+change+in+phosphorylation+status&sid=BE13A0E576A9FA1B1123BA5975278CCE.zQKnzAySRvJOZYcdfIziQ%3a760&sot=b&sdt=b&sl=139&s=TITLE-ABS-KEY%28The+conformational+change+of+a+murine+temperature-sensitive+p53+protein+is+independent+of+a+change+in+phosphorylation+status%29&origin=searchbasic&txGid=BE13A0E576A9FA1B1123BA5975278CCE.zQKnzAySRvJOZYcdfIziQ%3a76