Interaction of the Dr1 Inhibitory Factor with the TATA Binding Protein is Disrupted by Adenovirus E1A

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 91; no. 14; pp. 6279 - 6282
• Main Authors: Kraus, Virginia Byers, Inostroza, Juan A., Yeung, Kam, Reinberg, Danny, Nevins, Joseph R.
• Format: Journal Article
• Language: English
• Published: United States National Academy of Sciences of the United States of America 05.07.1994; National Acad Sciences; National Academy of Sciences
• Subjects: adenovirus; Adenovirus E1A Proteins - metabolism; Adenoviruses; Animals; Antibodies; Biochemistry; DNA-Binding Proteins - isolation & purification; DNA-Binding Proteins - metabolism; Drug interactions; Gels; Genetics; Glutathione Transferase - biosynthesis; Glutathione Transferase - metabolism; Goods and services tax; Heat-Shock Proteins - biosynthesis; Heat-Shock Proteins - metabolism; HeLa Cells; Humans; Luciferases - biosynthesis; Luciferases - metabolism; Phosphoproteins - isolation & purification; Phosphoproteins - metabolism; Plasmids; Proteins; Rabbits; Recombinant Fusion Proteins - biosynthesis; Recombinant Fusion Proteins - metabolism; TATA Box; TATA-Box Binding Protein; Transcription Factors - isolation & purification; Transcription Factors - metabolism; Transcription, Genetic; Transcriptional activation; Transfection
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.91.14.6279

Past experiments have shown that the adenovirus E1A12Sproduct activates the hsp70 promoter, dependent on the TATA element and dependent on N-terminal E1A sequences. Other experiments have identified a factor termed Dr1 that interacts with and inhibits the transcriptional activity of the TATA-binding protein (TBP). We now find that the E1A12Sprotein can disrupt the interaction of the Dr1 factor with the TATA-specific TBP factor, allowing the productive interaction of TBP with TFIIA. This E1A-mediated disruption is dependent on N-terminal sequences that are also essential for the TATA-dependent trans-activation of the hsp70 promoter. Moreover, we also find that Dr1 expression in transfected cells can inhibit transcription from the hsp70 promoter and that this can be overcome by coexpression of the wild-type E1A protein, dependent on N-terminal sequences. We conclude that the activation of hsp70 through the TATA element may be mechanistically similar to the activation of the E2 promoter via E2F, in each case involving a release of a transcription factor from an inactive complex.