Characterization of a p53 Regulatory Domain
Abstract
Our purpose is to characterize the proposed p53 regulatory domain and identify kinase(s) that may be involved in the regulation. Since 7/1/98, we have constructed a set of Gal4-p53N mutations and shown that mutants p53(DELTA 92-109), p53(DELTA ll7/128) and p53(S117/127A) 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 p53(DELTA 92-109), p53(DELTA 117-128) and p53(Sl17/l27A) 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 p53(S1l7/127A) displayed decreased protein levels, suggesting that serine residues 117/127 may play a role in stabilizing p53.
Document Details
- Document Type
- Technical Report
- Publication Date
- Jul 01, 1999
- Accession Number
- ADA386507
Entities
People
- Brian C. Abela
- Xuan Liu
Organizations
- University of California, Riverside