p53 and SV40 T antigen bind to the same region overlapping the conserved domain of the TATA-binding protein

• Published in: Biochemical and biophysical research communications Vol. 195; no. 1; p. 428
• Main Authors: Martin, D W, Subler, M A, Muñoz, R M, Brown, D R, Deb, S P, Deb, S
• Format: Journal Article
• Language: English
• Published: United States 31-08-1993
• Subjects: Amino Acid Sequence; Antigens, Polyomavirus Transforming - isolation & purification; Antigens, Polyomavirus Transforming - metabolism; Binding Sites; Conserved Sequence; DNA-Binding Proteins - biosynthesis; DNA-Binding Proteins - isolation & purification; DNA-Binding Proteins - metabolism; Gene Expression; Humans; Mutagenesis; Recombinant Proteins - biosynthesis; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; Restriction Mapping; Sequence Deletion; Simian virus 40 - metabolism; TATA Box; TATA-Box Binding Protein; Transcription Factors - biosynthesis; Transcription Factors - isolation & purification; Transcription Factors - metabolism; Transcription, Genetic; Tumor Suppressor Protein p53 - isolation & purification; Tumor Suppressor Protein p53 - metabolism
• ISSN: 0006-291X
• DOI: 10.1006/bbrc.1993.2061

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.