Mutants of Saccharomyces cerevisiae lacking activity of the Ca2+/calmodulin-dependent protein phosphatase calcineurin, show sensitivity to high concentrations of sodium that is partly reversed by the external supply of Ca2+. On long-time exposure to NaCl stress the mutants display an increased intracellular Na+/K+ ratio which is partially corrected by the addition of Ca2+, improving the sodium efflux of not only calcineurin-defective cells but also wild-type cells. We also demonstrate that the NaCl sensitivity of cmd mutants, expressing modified forms of calmodulin that do not bind Ca2+, is strongly reversed by the addition of Ca2+. This effect is highly dependent on calcineurin, since the NaCl tolerance of a cmd1-3 strain, carrying an additional mutation in calcineurin, is only slightly assisted by Ca2+. A striking characteristic of the loss of function of calcineurin is a several-fold increased content of intracellular Ca2+, localized mainly in subcellular compartment(s). If the compartmentalized Ca2+ pool is brought back to normal levels by an additional inactivating mutation of the vacuolar Ca2+-transporting ATPase, such double mutants do not significantly improve their tolerance to NaCl.
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Evidence ID | Analyze ID | Gene/Complex | Systematic Name/Complex Accession | Qualifier | Gene Ontology Term ID | Gene Ontology Term | Aspect | Annotation Extension | Evidence | Method | Source | Assigned On | Reference |
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Complement ID | Locus ID | Gene | Species | Gene ID | Strain background | Direction | Details | Source | Reference |
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Evidence ID | Analyze ID | Dataset | Description | Keywords | Number of Conditions | Reference |
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