SGD Paper 
Garbett KA, et al. (2007) Yeast TFIID serves as a coactivator for Rap1p by direct protein-protein interaction. Mol Cell Biol 27(1):297-311
Abstract: In vivo studies have previously shown that Saccharomyces cerevisiae ribosomal protein (RP) gene expression is controlled by transcription factor 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 map the domains of Rap1p and subunits of TFIID responsible. In vitro transcription of a UASRAP1-enhancer-driven reporter gene requires both Rap1p and TFIID and is independent of the Fhl1p-Ifh1p co-regulator. UASRAP1-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 TBP. We conclude that Rap1p and TFIID directly interact, and that this interaction contributes importantly to RP gene transcription.
| Status: Published | Type: Journal Article | PubMed ID: 17074814 |
Topics addressed in this paper
Number of different genes curated to this paper: 8
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