Schistosoma mansoni Ca2+-ATPase SMA2 Restores Viability to Yeast Ca2+-ATPase-deficient Strains and Functions in Calcineurin-mediated Ca2+Tolerance

The sarco(endo)plasmic reticulum of animal cells contains an ATP-powered Ca2+ pump that belongs to the P-type family of membrane-bound cation-translocating enzymes. InSchistosoma mansoni, the sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) is encoded by the SMA1 and SMA2 genes. A full-length SMA2 c...

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Bibliographic Details
Published in:The Journal of biological chemistry 1998-10, Vol.273 (43), p.27831-27840
Main Authors: Talla, Emmanuel, de Mendonça, Ricardo Luis, Degand, Ingrid, Goffeau, André, Ghislain, Michel
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Animals
Calcineurin - metabolism
Calcium - pharmacology
Calcium-Transporting ATPases - genetics
Calcium-Transporting ATPases - metabolism
Cell Compartmentation
Cloning, Molecular
DNA, Complementary - genetics
Drug Resistance
Genes, Helminth
Genetic Complementation Test
Intracellular Membranes - enzymology
Isoenzymes
Molecular Sequence Data
Rabbits
Saccharomyces cerevisiae - genetics
Sarcoplasmic Reticulum - enzymology
Schistosoma mansoni - enzymology
Sequence Analysis, DNA
Sequence Homology, Amino Acid
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Summary:The sarco(endo)plasmic reticulum of animal cells contains an ATP-powered Ca2+ pump that belongs to the P-type family of membrane-bound cation-translocating enzymes. InSchistosoma mansoni, the sarco(endo)plasmic reticulum Ca2+-ATPase (SERCA) is encoded by the SMA1 and SMA2 genes. A full-length SMA2 cDNA clone was isolated, sequenced, and expressed into a yeast Ca2+-ATPase-deficient strain requiring plasmid-borne rabbit SERCA1a for viability. The S. mansoniCa2+-ATPase supports growth of mutant cells lacking SERCA1a, indicating functional expression in yeast and a role in calcium sequestration. Subcellular fractionation showed that the SMA2 ATPase is localized in yeast internal membranes. SMA2 expression was found to be associated with thapsigargin-sensitive, Ca2+-dependent ATPase activity. The activity increased 2-fold upon calcineurin inactivation, which correlates within vivo stimulated contribution of SMA2 in calcium tolerance. These results suggest that calcineurin controls calcium homeostasis by inhibiting Ca2+-ATPase activity in an internal compartment.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.273.43.27831