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Characterization of physical interactions of the putative transcriptional adaptor, ADA2, with acidic activation domains and TATA-binding protein
UMass Chan Affiliations
Department of Medicine, Division of Infectious Diseases and ImmunologyDocument Type
Journal ArticlePublication Date
1995-08-18Keywords
*CCAAT-Binding FactorDNA-Binding Proteins
Fungal Proteins
Promoter Regions, Genetic
Protein Binding
Protein Kinases
*Saccharomyces cerevisiae Proteins
*TATA Box
TATA-Box Binding Protein
Trans-Activators
Transcription Factors
Immunology and Infectious Disease
Metadata
Show full item recordAbstract
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.Source
J Biol Chem. 1995 Aug 18;270(33):19337-44. Link to article on publisher's siteDOI
10.1074/jbc.270.33.19337Permanent Link to this Item
http://hdl.handle.net/20.500.14038/35023PubMed ID
7642611Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.1074/jbc.270.33.19337
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