Wild-type but not mutant p53 immunopurified proteins bind to sequences adjacent to the SV40 origin of replication. |
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Authors: | J Bargonetti P N Friedman S E Kern B Vogelstein C Prives |
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Institution: | Department of Biological Sciences, Columbia University, New York, New York 10027. |
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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. |
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