ApiLoc - A database of published protein sub-cellular localisation in Apicomplexa
|version 3 (curated until May 28, 2011)|
Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum.
Gunther, S., Wallace, L., Patzewitz, E. M., McMillan, P. J., Storm, J., Wrenger, C., Bissett, R., Smith, T. K., Muller, S. (2007 Dec, PLoS Pathog)
Lipoic acid (LA) is an essential cofactor of alpha-keto acid dehydrogenase complexes (KADHs) and the glycine cleavage system. In Plasmodium, LA is attached to the KADHs by organelle-specific lipoylation pathways. Biosynthesis of LA exclusively occurs in the apicoplast, comprising octanoyl-[acyl carrier protein]: protein N-octanoyltransferase (LipB) and LA synthase. Salvage of LA is mitochondrial and scavenged LA is ligated to the KADHs by LA protein ligase 1 (LplA1). Both pathways are entirely independent, suggesting that both are likely to be essential for parasite survival. However, disruption of the LipB gene did not negatively affect parasite growth despite a drastic loss of LA (>90%). Surprisingly, the sole, apicoplast-located pyruvate dehydrogenase still showed lipoylation, suggesting that an alternative lipoylation pathway exists in this organelle. We provide evidence that this residual lipoylation is attributable to the dual targeted, functional lipoate protein ligase 2 (LplA2). Localisation studies show that LplA2 is present in both mitochondrion and apicoplast suggesting redundancy between the lipoic acid protein ligases in the erythrocytic stages of P. falciparum.
PFI1160w (LplA2) lipoate protein ligase a type 2Experimental localisation: mitochondrion during ring, mitochondrion during trophozoite, mitochondrion during schizont, mitochondrion during merozoite, apicoplast during ring, apicoplast during trophozoite, apicoplast during schizont, apicoplast during merozoite
PF08_0066 (aLipDH) lipoamide dehydrogenaseExperimental localisation: apicoplast during intraerythrocytic, not mitochondrion during intraerythrocytic