Complementation of Saccharomyces cerevisiaepik1ts by a phosphatidylinositol 4-kinase from Plasmodium falciparum

• Published in: Molecular and biochemical parasitology 2010-08, Vol.172 (2), p.149-151
• Main Authors: Krüger, Tim, Sanchez, Cecilia P., Lanzer, Michael
• Format: Article
• Language: English
• Subjects: 1-Phosphatidylinositol 4-Kinase - deficiency; 1-Phosphatidylinositol 4-Kinase - genetics; Complementation; Genetic Complementation Test; Hot Temperature; Kinase; Mutation, Missense; P. falciparum; Phosphoinositides; Plasmodium falciparum - enzymology; Plasmodium falciparum - genetics; Protozoan Proteins - genetics; Saccharomyces cerevisiae - enzymology; Saccharomyces cerevisiae - genetics; Saccharomyces cerevisiae Proteins - genetics
• ISSN: 0166-6851; 1872-9428
• DOI: 10.1016/j.molbiopara.2010.03.020

The Plasmodium falciparum gene PFE0485w can functionally complement the temperature sensitive pik1 mutation in yeast, suggesting that PFE0485w encodes a phosphatidylinositol 4-kinase. Phosphoinositides comprise a group of essential phospholipids that control a variety of cellular functions. In the case of the human malaria parasite Plasmodium falciparum, phosphoinositides have been shown to trigger exflagellation and to affect haemoglobin endocytosis and maturation of the parasite's digestive vacuole. A central enzyme in the formation of phosphoinositides is the phosphatidylinositol 4-kinase that catalyzes the production of phosphatidylinositol 4-phosphate from phosphatidylinositol. Here we have identified and characterized a phosphatidylinositol 4-kinase from P. falciparum. Our data show that the corresponding P. falciparum gene, termed PFE0485w, can functionally complement a yeast temperature-sensitive pik1 mutation. Our data add to the concept that P. falciparum maintains its own phospholipids biosynthesis pathway.