Plasma-membrane ATPase action affects several stress tolerances of Saccharomyces cerevisiae and Schizosaccharomyces pombe as well as the extent and duration of the heat shock response
The pma1.1 mutations of Saccharomyces cerevisiae and Schizosaccharomyces pombe decrease plasma-membrane ATPase activity. This study investigated how they affect different stress tolerances, and the extent and duration of the heat-shock response. pma1.1 mutants exhibited higher resistance to ethanol and osmotic stress, but lower tolerance to ultraviolet damage, as compared to wild-type cells. pma1.1 mutations also increased tolerance of the lethal temperature of 48 °C in cells in which no heat-shock response had been induced. However, after induction of a heat-shock response and elevated thermotolerance by a 25–38 °C upshift, then maintaining cells at 38 °C for 40 min, pma1.1 lowered subsequent tolerances of much higher lethal temperatures. Analysis of pulse-labelled S. cerevisiae proteins revealed reduced heat-shock protein synthesis in the pma1.1 mutant after a 25–38 °C heat shock. This may explain the greater increases in thermotolerance in wild-type as compared to pma1.1 cells after both were given identical 25–38 °C shocks. With more severe treatment (25–42 °C), heat-shock protein synthesis in wild-type cells, although initially high, was switched off more rapidly than in the pma1.1 mutant. These results indicate that plasma-membrane ATPase action exerts a major influence over several stress tolerances, as well as the extent and duration of heat-shock protein synthesis following induction of the heat-shock response.
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Plasma-membrane ATPase action affects several stress tolerances of Saccharomyces cerevisiae and Schizosaccharomyces pombe as well as the extent and duration of the heat shock response