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J. Biol. Chem., Vol. 268, Issue 18, 13062-13067, Jun, 1993
DW Martin, RM Munoz, MA Subler and S Deb
Earlier reports show that p53, both wild type and mutants, may affect
transcription. Wild-type p53 activates promoters with p53-binding sites
while inhibiting promoters without binding sites. Mutant p53, on the other
hand, has been shown to activate transcription from specific promoters.
These observations suggest that both wild-type and mutant p53 may interact
with a general transcription factor(s). In this report, we have shown that
the cloned TATA-binding protein (TBP) from human and yeast interacts with
human p53. TBP co-immunoprecipitates with wild-type or mutant human p53
when incubated with the p53-specific monoclonal antibody and Protein
A-agarose. Wild-type murine p53 has also been found to interact with human
TBP. Protein blot assays have demonstrated that the interaction between p53
and human TBP is direct. By gel retention analysis, we have shown that the
complex of TBP and p53 (both wild type and mutant) can bind to the TATA
box. The similar qualitative binding capability of wild-type and mutant p53
with human TBP and the similarity of the two complexes in binding to the
TATA box suggest that the functional discrimination between wild-type and
mutant p53 may not lie in their ability to bind TBP. The nature of the
p53.TBP or p53.TBP.TATA complex may determine the success of transcription.
p53 binds to the TATA-binding protein-TATA complex
Department of Microbiology, University of Texas Health Science Center, San Antonio 78284.
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