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

Jill Bargonetti, Paula N. Friedman, Scott E Kern, Bert Vogelstein, Carol Prives

Research output: Contribution to journalArticle

Abstract

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.

Original languageEnglish (US)
Pages (from-to)1083-1091
Number of pages9
JournalCell
Volume65
Issue number6
DOIs
StatePublished - Jun 14 1991

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ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

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