The TBP-TFIIA interaction in the response to acidic activators in vivo.
A yeast TBP mutant (N2-1) is described here that is defective specifically in responding to acidic activators in vivo. N2-1 does not support activation by Gal4, Ace1, and Gcn4, but appears unaffected for constitutive transcription, repression by the Cyc8-Tup1 and Not complexes, and transcription by polymerase I (Pol) and Pol ... III. In vitro, N2-1 fails to interact with TFIIA, but it associates normally with a TATA element, an acidic activation domain, and TFIIB. Fusion of the small subunit of TFIIA to N2-1 restores activation function in vivo. Thus, an efficient interaction between TBP and TFIIA is required for transcriptional activation in vivo.
Mesh Terms:
Base Sequence, DNA-Binding Proteins, DNA-Directed RNA Polymerases, Fungal Proteins, Hydrogen-Ion Concentration, Immediate-Early Proteins, Molecular Sequence Data, Mutation, Nuclear Proteins, Nuclear Receptor Subfamily 4, Group A, Member 2, Protein Kinases, Repressor Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, TATA Box, TATA-Box Binding Protein, Trans-Activators, Transcription Factor TFIIA, Transcription Factors, Transcriptional Activation
Base Sequence, DNA-Binding Proteins, DNA-Directed RNA Polymerases, Fungal Proteins, Hydrogen-Ion Concentration, Immediate-Early Proteins, Molecular Sequence Data, Mutation, Nuclear Proteins, Nuclear Receptor Subfamily 4, Group A, Member 2, Protein Kinases, Repressor Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, TATA Box, TATA-Box Binding Protein, Trans-Activators, Transcription Factor TFIIA, Transcription Factors, Transcriptional Activation
Science
Date: Jul. 07, 1995
PubMed ID: 7604282
View in: Pubmed Google Scholar
Download Curated Data For This Publication
17593
Switch View:
- Interactions 1