ArticleThe Biochemical journal2011
Overexpression of a cytosolic pyrophosphatase (TgPPase) reveals a regulatory role of PP(i) in glycolysis for Toxoplasma gondii.
Article in The Biochemical journal, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 20 citations in OpenAlex.
- Article
- HParasitology research · 2024Review
- Review
- Plasmodium falciparum utilizes pyrophosphate to fuel an essential proton pump in the ring stage and the transition to trophozoite stage.PLoS pathogens · 2023Article
- Essential role of pyrophosphate homeostasis mediated by the pyrophosphate-dependent phosphofructokinase in Toxoplasma gondii.PLoS pathogens · 2022Article
- Crystal Structure of Inorganic Pyrophosphatase FromFrontiers in cell and developmental biology · 2021Article
- A single Na+-Pi cotransporter in Toxoplasma plays key roles in phosphate import and control of parasite osmoregulation.PLoS pathogens · 2020Article
- The Toxoplasma Vacuolar HCell reports · 2019Article
- Associations of canopy leaf traits with SNP markers in durum wheat (Triticum turgidum L. durum (Desf.)).PloS one · 2018Article
- A CTP Synthase Undergoing Stage-Specific Spatial Expression Is Essential for the Survival of the Intracellular ParasiteFrontiers in cellular and infection microbiology · 2018Article
- Structural and Biochemical Characterization of Apicomplexan Inorganic Pyrophosphatases.Scientific reports · 2017Article
- A vacuolar-H(+) -pyrophosphatase (TgVP1) is required for microneme secretion, host cell invasion, and extracellular survival of Toxoplasma gondii.Molecular microbiology · 2014Article
- Toxoplasma gondii relies on both host and parasite isoprenoids and can be rendered sensitive to atorvastatin.PLoS pathogens · 2013Article
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5 authors at 1 institution in 1 country.
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Abstract
PP(i) is a critical element of cellular metabolism as both an energy donor and as an allosteric regulator of several metabolic pathways. The apicomplexan parasite Toxoplasma gondii uses PP(i) in place of ATP as an energy donor in at least two reactions: the glycolytic PP(i)-dependent PFK (phosphofructokinase) and V-H(+)-PPase [vacuolar H(+)-translocating PPase (pyrophosphatase)]. In the present study, we report the cloning, expression and characterization of cytosolic TgPPase (T. gondii soluble PPase). Amino acid sequence alignment and phylogenetic analysis indicates that the gene encodes a family I soluble PPase. Overexpression of the enzyme in extracellular tachyzoites led to a 6-fold decrease in the cytosolic concentration of PP(i) relative to wild-type strain RH tachyzoites. Unexpectedly, this subsequent reduction in PP(i) was associated with a higher glycolytic flux in the overexpressing mutants, as evidenced by higher rates of proton and lactate extrusion. In addition to elevated glycolytic flux, TgPPase-overexpressing tachyzoites also possessed higher ATP concentrations relative to wild-type RH parasites. These results implicate PP(i) as having a significant regulatory role in glycolysis and, potentially, other downstream processes that regulate growth and cell division.
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