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

Abstract:

: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.

journal_name

Mol Biochem Parasitol

authors

Krüger T,Sanchez CP,Lanzer M

doi

10.1016/j.molbiopara.2010.03.020

subject

Has Abstract

pub_date

2010-08-01 00:00:00

pages

149-51

issue

2

eissn

0166-6851

issn

1872-9428

pii

S0166-6851(10)00071-X

journal_volume

172

pub_type

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