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Rabbit sarcoplasmic reticulum Ca 2+ ‐ATPase replaces yeast PMC1 and PMR1 Ca 2+ ‐ATPases for cell viability and calcineurin‐dependent regulation of calcium tolerance
Author(s) -
Degand Ingrid,
Catty Patrice,
Talla Emmanuel,
ThinèsSempoux D.,
De Kerchove d'Exaerde Alban,
Goffeau André,
Ghislain Michel
Publication year - 1999
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1046/j.1365-2958.1999.01195.x
Subject(s) - endoplasmic reticulum , biology , atpase , calcium atpase , plasma membrane ca2+ atpase , golgi apparatus , microbiology and biotechnology , calcium , calcineurin , biochemistry , intracellular , vacuole , saccharomyces cerevisiae , yeast , enzyme , chemistry , medicine , cytoplasm , organic chemistry , transplantation
SERCA1a, the fast‐twitch skeletal muscle isoform of sarco(endo)plasmic reticulum Ca 2+ ‐ATPase, was expressed in yeast using the promoter of the plasma membrane H + ‐ATPase. In the yeast Saccharomyces cerevisiae , the Golgi PMR1 Ca 2+ ‐ATPase and the vacuole PMC1 Ca 2+ ‐ATPase function together in Ca 2+ sequestration and Ca 2+ tolerance. SERCA1a expression restored growth of pmc1 mutants in media containing high Ca 2+ concentrations, consistent with increased Ca 2+ uptake in an internal compartment. SERCA1a expression also prevented synthetic lethality of pmr1 pmc1 double mutants on standard media. Electron microscopy and subcellular fractionation analysis showed that SERCA1a was localized in intracellular membranes derived from the endoplasmic reticulum. Finally, we found that SERCA1a ATPase activity expressed in yeast was regulated by calcineurin, a Ca 2+ /calmodulin‐dependent phosphoprotein phosphatase. This result indicates that calcineurin contributes to calcium homeostasis by modulating the ATPase activity of Ca 2+ pumps localized in intracellular compartments.