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doi:10.1534/genetics.105.043109
A more recent version of this article appeared on July 1, 2005.
REGULAR RESEARCH PAPERS |
The molecular chaperone Sse1 and the growth control protein kinase Sch9 collaborate to regulate protein kinase A activity in Saccharomyces cerevisiae
Amy Trott 1, Lance Shaner 1 and Kevin Morano 1*
1 University of Texas Medical School
* To whom correspondence should be addressed. E-mail: kevin.a.morano{at}uth.tmc.edu.
Submitted on March 9, 2005
Revised on March 15, 2005
Accepted on 15 March 2005
The Sch9 protein kinase regulates Hsp90-dependent signal transduction activity in the budding yeast Saccharomyces cerevisiae. Hsp90 functions in concert with a number of co-chaperones, including the Hsp110 homolog Sse1. In this report, we demonstrate a novel synthetic genetic interaction between SSE1 and SCH9. This interaction was observed specifically during growth at elevated temperature, and was suppressed by decreased signaling through the protein kinase A (PKA) signal transduction pathway. Correspondingly, sse1
sch9 cells were shown by both genetic and biochemical approaches to have abnormally high levels of PKA activity and were less sensitive to modulation of PKA by glucose availability. Growth defects of an sse1 mutant were corrected by reducing PKA signaling through overexpression of negative regulators or growth on non-optimal carbon sources. Hyper-activation of the PKA pathway through expression of a constitutive RAS2 allele likewise resulted in temperature sensitive growth, suggesting that modulation of PKA activity during thermal stress is required for adaptation and viability. Together these results demonstrate that the Sse1 chaperone and the growth control kinase Sch9 independently contribute to regulation of PKA signaling.
Key Words: Saccharomyces, protein chaperone, protein kinase A, signal transduction
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