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Yeast Whi2 and Psr1-phosphatase form a complex and regulate STRE-mediated gene expression
Daisuke Kaida1, Hideki Yashiroda, Akio Toh-e
1Department of Biological Sciences, Graduate School of Science, The University of Tokyo, Japan.
Summary
The Whi2 protein and its partner, Psr1 phosphatase, are crucial for activating the general stress response in yeast. This interaction, possibly via Msn2 dephosphorylation, influences cell size and stress adaptation.
Area of Science:
- Molecular Biology
- Cellular Stress Response
- Yeast Genetics
Background:
- The general stress response in Saccharomyces cerevisiae involves Msn2 and Msn4 transcription factors inducing STRE-mediated gene expression.
- WHI2 cells exhibit smaller size in stationary phase compared to wild-type cells.
Purpose of the Study:
- To investigate the role of WHI2 in the general stress response.
- To identify WHI2-interacting proteins and elucidate their function in stress adaptation.
Main Methods:
- Two-hybrid system to identify WHI2-interacting genes.
- Analysis of STRE-mediated gene expression under stress conditions.
- Co-immunoprecipitation to confirm protein interactions.
Main Results:
- STRE-mediated gene expression was reduced by half and delayed in whi2 cells.
- WHI2-interacting gene PSR1, encoding a plasma membrane phosphatase, was identified.
- whi2 and psr1 psr2 mutants showed similar phenotypes, including sensitivity to stress and Msn2 hyper-phosphorylation.
- Psr1 phosphatase activity and Whi2-Psr1 interaction were essential for full STRE activation.
Conclusions:
- Whi2 and Psr1 phosphatase are required for the full activation of the general stress response in yeast.
- The Whi2-Psr1 complex may regulate the general stress response through Msn2 dephosphorylation.
- These findings provide a molecular explanation for the smaller cell size observed in stationary phase whi2 cells.