A plasma membrane-type Ca2+-ATPase co-localizes with a vacuolar H+-pyrophosphatase to acidocalcisomes of Toxoplasma gondii

摘要: Ca2+-ATPases are likely to play critical roles in the biochemistry of Toxoplasma gondii, since these protozoa obligate intracellular parasites and Ca2+ concentration their location is three orders magnitude lower than extracellular medium. Here, we report cloning sequencing a gene encoding plasma membrane-type Ca2+-ATPase (PMCA) T.gondii (TgA1). The predicted protein (TgA1) exhibits 32–36% identity vacuolar Trypanosoma cruzi, Saccharomyces cerevisiae, Entamoeba histolytica Dictyostelium discoideum. Sequencing both cDNA genomic DNA from indicated that TgA1 contains two introns near C-terminus. A hydropathy profile suggests 10 transmembrane domains. suppresses hypersensitivity mutant S.cerevisiae has defect accumulation. Indirect immunofluorescence immunoelectron microscopy analysis indicate localizes membrane co-localizes with H+-pyrophosphatase vacuoles identified morphologically by X-ray microanalysis as acidocalcisomes. This vacuolar-type could an important role homeostasis T.gondii.