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


Name: Chang, Ya-Wen
Mailing Address: Molecular Genetics, The Ohio State University, 484 W.12th Ave., Columbus, OH 43210, USA
Email Address: chang.364@osu.edu
Phone & FAX numbers: (614)688-5499 & (614)292-4466

Abstract #50


Session Title: Transcription, Elongation and Termination
Session Time: Friday, August 2 -- 11:00AM - 12:30PM
Presentation: Platform
Topic: Gene Expression

The Ras/PKA pathway controls gene expression by regulating the activity of Srb complex proteins present in the RNA pol II holoenzyme.
Ya-Wen Chang, Paul K. Herman
Molecular Genetics, The Ohio State University, 484 W.12th Ave., Columbus, OH 43210, USA

Upon nutrient deprivation, S. cerevisiae cells arrest division and enter into a specialized resting state, known as stationary phase. The entry into this resting state is regulated in part by the Ras/PKA (cAMP-dependent protein kinase) signaling pathway. We are interested in defining the targets of PKA relevant for this growth control. To this end, we have identified a collection of rye mutants that are defective in the transcriptional response to nutrient deprivation and in stationary phase entry. Interestingly, three of these RYE genes have been shown to encode the Srb/Ssn proteins, Srb9p, Srb10p, and Srb11p. These Srb proteins are part of the Srb complex associated with the RNA polymerase II holoenzyme. We found that specific transcription defects associated with these srb mutations were suppressed by RAS2val19, a hyperactive allele of RAS2. However, increased Ras signaling was not able to correct the expression defects associated with an srb9 null mutant suggesting that the Srb9 protein is essential for the Ras suppression. Moreover, there are two potential PKA sites in Srb9p, and our results show that the suppression of the srb9 defects requires the presence of these two PKA sites. In addition, Srb9p is a phosphoprotein in vivo, and these two Srb9p sites are phosphorylated by PKA in vitro. In all, our results suggest that Srb9p is a substrate for PKA, and this phosphorylation of Srb9p modulates the in vivo activity of the Srb complex.


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