Characterization of a p53 Regulatory Domain
Annual rept. 1 Jul 1998-30 Jun 1999
CALIFORNIA UNIV RIVERSIDE
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Our purpose is to characterize the proposed p53 regulatory domain and identify kinases that may be involved in the regulation. Since 7198, we have constructed a set of Gal4-p53N mutations and shown that mutants p53DELTA 92-109, p53DELTA ll7128 and p53S117127A significantly lost their ability to activate transcription in vivo. We consider the possibility that failure to detect any transcription activity may be due to a loss of DNA-binding activity. To test this, a gel shift experiment was performed and our results showed that mutants p53DELTA 92-109, p53DELTA 117-128 and p53Sl17l27A all retained their abilities to bind to DNA. We next examined the p53 protein levels as wild-type p53 are known to be rapidly degraded in part through the ubiquitin pathway. Indeed, our results showed that p53S1l7127A displayed decreased protein levels, suggesting that serine residues 117127 may play a role in stabilizing p53.
- Medicine and Medical Research