p53 and SV40 T antigen bind to the same region overlapping the conserved domain of the TATA-binding protein.
In this report we demonstrate that the cloned human TATA-binding protein (TBP) interacts with T antigen. TBP co-immunoprecipitates with T antigen when incubated with the T antigen-specific monoclonal antibody PAb419, and Protein-A agarose. Gel retention analysis with a radiolabeled TATA box-containing probe showed that the complex of TBP and T ... antigen can bind to the TATA box. Recently, p53 has also been shown to interact with TBP. Using TBP deletion mutants and co-immunoprecipitation experiments with p53 or T antigen, we show that both p53 and T antigen bind to the same region, amino acids 203-275, within the conserved C-terminal domain of TBP. Binding of p53 and T antigen to the same domain on TBP may lead to competition between the two proteins for transcriptional function.
Mesh Terms:
Amino Acid Sequence, Antigens, Polyomavirus Transforming, Binding Sites, Conserved Sequence, DNA-Binding Proteins, Gene Expression, Humans, Mutagenesis, Recombinant Proteins, Restriction Mapping, Sequence Deletion, Simian virus 40, TATA Box, TATA-Box Binding Protein, Transcription Factors, Transcription, Genetic, Tumor Suppressor Protein p53
Amino Acid Sequence, Antigens, Polyomavirus Transforming, Binding Sites, Conserved Sequence, DNA-Binding Proteins, Gene Expression, Humans, Mutagenesis, Recombinant Proteins, Restriction Mapping, Sequence Deletion, Simian virus 40, TATA Box, TATA-Box Binding Protein, Transcription Factors, Transcription, Genetic, Tumor Suppressor Protein p53
Biochem. Biophys. Res. Commun.
Date: Aug. 31, 1993
PubMed ID: 8395834
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