Complementation of Saccharomyces cerevisiae pik1ts by a phosphatidylinositol 4-kinase from Plasmodium falciparum

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 parasit...

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Bibliographic Details
Main Authors: Krüger, Tim (Author) , Sanchez, Cecilia P. (Author) , Lanzer, Michael (Author)
Format: Article (Journal)
Language:English
Published: 8 April 2010
In: Molecular and biochemical parasitology
Year: 2010, Volume: 172, Issue: 2, Pages: 149-151
ISSN:1872-9428
DOI:10.1016/j.molbiopara.2010.03.020
Online Access:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.molbiopara.2010.03.020
Verlag, lizenzpflichtig, Volltext: https://www.sciencedirect.com/science/article/pii/S016668511000071X
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Author Notes:Tim Krüger, Cecilia P. Sanchez, Michael Lanzer
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Summary: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.
Item Description:Gesehen am 06.03.2023
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Physical Description:Online Resource
ISSN:1872-9428
DOI:10.1016/j.molbiopara.2010.03.020