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

Garbett KA, Tripathi MK, Cencki B, Layer JH, Weil PA
Mol Cell Biol. 2007 27 (1): 297-311

PMID: 17074814 · PMCID: PMC1800639 · DOI:10.1128/MCB.01558-06

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 (16)

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, Genetic Transcriptional Activation Transcription Factors Transcription Factor TFIID

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