Yeast Genetics and Molecular Biology 2002
University of Wisconsin
Madison, Wisconsin USA
July 30 - August 4, 2002


Name: Swanson, Mark J.
Mailing Address: LGRD/NICHD, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD 20892, USA
Email Address: swansonm@mail.nih.gov
Phone & FAX numbers: 301-594-7240 & 301-496-8576
URL: http://eclipse.nichd.nih.gov/nichd/lgrd/sncge/index.htm

Abstract #21


Session Title: Global Analysis of Gene Expression
Session Time: Wednesday, July 31 -- 2:00PM - 3:30PM
Presentation: Platform
Topic: Gene Expression

A comprehensive analysis of Gcn4p coactivator requirements reveals novel genetic and physical interactions.
Mark J. Swanson, Laarni Sumibcay, Anna Krueger, Soon-ja Kim, Fan Zhang, Hongfang Qiu, Alan G. Hinnebusch
LGRD/NICHD, National Institutes of Health, 9000 Rockville Pike, Bethesda, MD 20892, USA

Eukaryotic transcriptional regulation requires sequence specific DNA binding proteins to activate transcription from target genes organized in repressive chromatin. Activators recruit multisubunit coactivator complexes harboring activities to alter chromatin and recruit general transcription factors and RNA polII. Budding yeast cells respond to amino acid starvation by inducing Gcn4p, an activator of amino acid biosynthetic genes. Our previous studies showed that SAGA, SWI/SNF and SRB/MED coactivators can interact with Gcn4p in vitro, and mutations in subunits of these complexes decrease activation by Gcn4p in vivo. We are conducting a comprehensive analysis of Gcn4p coactivator requirements by testing all viable mutants from the Saccharomyces Deletion Project for defects in activation by Gcn4p in vivo. Our data confirm that Gcn4p requires SAGA, SWI/SNF and SRB/MED and identify key nonessential subunits in these complexes required for activation in vivo. We uncovered a strong dependence on CCR4/NOT and significant requirements for RSC, PAF1/mediator and TFIID. In vitro binding experiments suggest that Gcn4p interacts specifically with CCR4/NOT and RSC but not with TFIID or PAF1/mediator. Interaction assays reveal that deletions of certain SAGA and SRB/MED subunits with strong activation defects in vivo disrupt in vitro binding of Gcn4p to the complex; other deletions do not reduce in vitro binding to Gcn4p and may impair a biochemical function of the coactivator in vivo.


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