Wild-type but not mutant p53 immunopurified proteins bind to sequences adjacent to the SV40 origin of replication

作者：Jill Bargonetti, Paula N. Friedman, Scott E. Kern, Bert Vogelstein, Carol L. Prives · 发表于：Cell · 年份：1991 · DOI：10.1016/0092-8674(91)90560-l · 被引用次数：382 · 研究领域：Cancer-related Molecular Pathways、Virus-based gene therapy research、CRISPR and Genetic Engineering

The DNA from a wide variety of human tumors has sustained mutations within the conserved p53 coding regions. We have purified wild-type and tumor-derived mutant p53 proteins expressed from baculovirus vectors and examined their interactions with SV40 DNA. Using DNAase I footprinting assays, we observed that both human and murine wild-type p53 proteins bind specifically to sequences adjacent to the late border of the viral replication origin. By contrast, mutant p53 proteins failed to bind specifically to these sequences. SV40 T antigen prevented wild-type p53 from interacting with this region. These data show that normal but not oncogenic forms of p53 are capable of sequence-specific interactions with viral DNA. Furthermore, they provide insights into the mechanisms by which viral proteins might regulate the control of viral growth and cell division.