Premium
Yeast TFIID Serves as a Coactivator for Rap1p by Direct Protein‐Protein Interaction
Author(s) -
Weil P. Anthony,
Garbett Krassimira A.,
Tripathi Manish K.,
Layer Justin H.
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a656-b
Subject(s) - taf4 , transcription factor ii a , taf1 , coactivator , biology , microbiology and biotechnology , taf2 , transcription factor ii d , transcription factor , enhancer , genetics , gene , polymerase , gene expression , promoter , rna dependent rna polymerase
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. We have tested the hypothesis that yeast TFIID serves as a coactivator for RP gene transcription by directly interacting with Rap1p. We have observed that Rap1p sub‐stoichiometrically co‐purifies with TFIID from yeast extracts, 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 UAS RAP1 ‐enhancer‐driven reporter gene requires both Rap1p and TFIID, and is independent of the Fhl1p‐Ifh1p co‐regulator. UAS RAP1 ‐ enhancer‐driven transactivation in extracts depleted of both Rap1p and TFIID is efficiently rescued by addition of these two purified proteins but not TBP. We conclude that Rap1p and TFIID directly interact to drive transcription of the RP genes.