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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| Main Authors: | , , |
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| Format: | Article (Journal) |
| Language: | English |
| Published: |
8 April 2010
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| 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 |
| Author Notes: | Tim Krüger, Cecilia P. Sanchez, Michael Lanzer |
| 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. |
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| Item Description: | Gesehen am 06.03.2023 Im Titel sind die Buchstaben "ts" hochgestellt |
| Physical Description: | Online Resource |
| ISSN: | 1872-9428 |
| DOI: | 10.1016/j.molbiopara.2010.03.020 |