Yeast TFIID serves as a coactivator for Rap1p by direct protein-protein interaction.

In vivo studies have previously shown that Saccharomyces cerevisiae ribosomal protein (RP) gene expression is controlled by the transcription factor repressor activator protein 1 (Rap1p) in a TFIID-dependent fashion. Here we have tested the hypothesis that yeast TFIID serves as a coactivator for RP gene transcription by directly interacting with ...
Rap1p. We have found that purified recombinant Rap1p specifically interacts with purified TFIID in pull-down assays, and we have mapped the domains of Rap1p and subunits of TFIID responsible. In vitro transcription of a UAS(RAP1) enhancer-driven reporter gene requires both Rap1p and TFIID and is independent of the Fhl1p-Ifh1p coregulator. UAS(RAP1) enhancer-driven transactivation in extracts depleted of both Rap1p and TFIID is efficiently rescued by addition of physiological amounts of these two purified factors but not TATA-binding protein. We conclude that Rap1p and TFIID directly interact and that this interaction contributes importantly to RP gene transcription.
Mesh Terms:
Binding, Competitive, DNA-Binding Proteins, Enhancer Elements, Genetic, Gene Expression Regulation, Fungal, Protein Binding, Protein Interaction Mapping, Protein Structure, Tertiary, Recombinant Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, TATA-Box Binding Protein, Telomere-Binding Proteins, Transcription Factor TFIID, Transcription Factors, Transcription, Genetic, Transcriptional Activation
Mol. Cell. Biol.
Date: Jan. 01, 2007
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