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Article
Characterization of physical interactions of the putative transcriptional adaptor, ADA2, with acidic activation domains and TATA-binding protein
Infectious Diseases and Immunology Publications and Presentations
  • Nickolai A. Barlev, Wistar Institute
  • Reyes Candau, Wistar Institute
  • Lian Wang, Wistar Institute
  • Paula Darpino, Wistar Institute
  • Neal S. Silverman, University of Massachusetts Medical School
  • Shelley L. Berger, Wistar Institute
UMMS Affiliation
Department of Medicine, Division of Infectious Diseases and Immunology
Date
8-18-1995
Document Type
Article
Subjects
*CCAAT-Binding Factor; DNA-Binding Proteins; Fungal Proteins; Promoter Regions, Genetic; Protein Binding; Protein Kinases; *Saccharomyces cerevisiae Proteins; *TATA Box; TATA-Box Binding Protein; Trans-Activators; Transcription Factors
Abstract
RNA polymerase II transcription requires functional interactions between activator proteins bound to upstream DNA sites and general factors bound to the core promoter. Accessory transcription factors, such as adaptors and coactivators, have important, but still unclear, roles in the activation process. We tested physical interactions of the putative adaptor ADA2 with activation domains derived from acidic activator proteins and with certain general transcription factors. ADA2 associated with the herpesvirus VP16 and yeast GCN4 activation domains but not with the activation domain of yeast HAP4, which previously was shown to be independent of ADA2 function in vivo and in vitro. Furthermore, the amino terminus of ADA2 directly interacted with the VP16 activation domain, suggesting that ADA2 provides determinants for interaction between activation domains and the adaptor complex. Both TATA-binding protein (TBP) and TFIIB have previously been shown to interact directly with the VP16 activation domain in vitro (Stringer, K. F., Ingles, C. J., and Greenblatt, J. (1990) Nature 345, 783-786; Lin, Y. S., Ha, I., Maldonado, E., Reinberg, D., and Green, M. R. (1991) Nature 353, 569-571). Interestingly, when binding was tested between VP16 and these general factors in yeast nuclear extracts, both factors interacted with VP16, but only the TBP/VP16 association was dependent on ADA2. In addition, ADA2 physically associated with TBP, but not with TFIIB. These results suggest that the role of ADA2 in transcriptional activation is to promote physical interaction between activation domains and TBP.
Rights and Permissions
Citation: J Biol Chem. 1995 Aug 18;270(33):19337-44. Link to article on publisher's site
Related Resources
Link to Article in PubMed
PubMed ID
7642611
Citation Information
Nickolai A. Barlev, Reyes Candau, Lian Wang, Paula Darpino, et al.. "Characterization of physical interactions of the putative transcriptional adaptor, ADA2, with acidic activation domains and TATA-binding protein" Vol. 270 Iss. 33 (1995) ISSN: 0021-9258 (Print)
Available at: http://works.bepress.com/neal_silverman/14/