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

Cell. 1991 Jun 14;65(6):1083-91. doi: 10.1016/0092-8674(91)90560-l.

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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Antigens, Polyomavirus Transforming / metabolism*
  • DNA Mutational Analysis
  • DNA Replication*
  • DNA, Viral / metabolism
  • DNA-Binding Proteins / metabolism*
  • In Vitro Techniques
  • Mice
  • Recombinant Proteins / metabolism
  • Regulatory Sequences, Nucleic Acid*
  • Simian virus 40 / genetics*
  • Tumor Suppressor Protein p53 / genetics
  • Tumor Suppressor Protein p53 / metabolism*
  • Virus Replication*

Substances

  • Antigens, Polyomavirus Transforming
  • DNA, Viral
  • DNA-Binding Proteins
  • Recombinant Proteins
  • Tumor Suppressor Protein p53