Related Experiment Video
Updated: Jul 19, 2026

Development and Application of Rapamycin-regulated Tyrosine Phosphatases
Published on: September 6, 2024
Yeast TFIID serves as a coactivator for Rap1p by direct protein-protein interaction
Krassimira A Garbett1, Manish K Tripathi, Belgin Cencki
1Department of Molecular Physiology and Biophysics, Vanderbilt University, School of Medicine, Nashville, TN 37232-0615, USA.
Abstract:
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.
More Related Videos
11:25Enhanced Yeast One-hybrid Screens To Identify Transcription Factor Binding To Human DNA Sequences
Published on: February 11, 2019
09:21Saccharomyces cerevisiae Metabolic Labeling with 4-thiouracil and the Quantification of Newly Synthesized mRNA As a Proxy for RNA Polymerase II Activity
Published on: October 22, 2018
Related Concept Videos
Yeast Signaling
Tail-anchoring of Proteins in the ER Membrane
RNA Polymerase II Accessory Proteins
RNA Polymerase II Accessory Proteins
tRNA Activation
tRNA Activation