p53 binds to the TATA-binding protein-TATA complex

• Published in: The Journal of biological chemistry 1993-06, Vol.268 (18), p.13062-13067
• Main Authors: MARTIN, D. W, MUNOZ, R. M, SUBLER, M. A, DEB, S
• Format: Article
• Language: English
• Subjects: Animals; Baculoviridae - genetics; Base Sequence; Binding Sites; Biological and medical sciences; Cell Line; Cloning, Molecular; DNA-Binding Proteins - genetics; DNA-Binding Proteins - isolation & purification; DNA-Binding Proteins - metabolism; Fundamental and applied biological sciences. Psychology; Humans; Mice; Molecular and cellular biology; Molecular genetics; Molecular Sequence Data; Oligodeoxyribonucleotides; Precipitin Tests; Saccharomyces cerevisiae - metabolism; TATA Box; TATA-Box Binding Protein; Transcription Factors - genetics; Transcription Factors - isolation & purification; Transcription Factors - metabolism; Transcription. Transcription factor. Splicing. Rna processing; Tumor Suppressor Protein p53 - genetics; Tumor Suppressor Protein p53 - isolation & purification; Tumor Suppressor Protein p53 - metabolism
• ISSN: 0021-9258; 1083-351X
• DOI: 10.1016/s0021-9258(19)38619-3

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.