Figure 4 | Scientific Reports

Figure 4

From: Structure, Function and Inhibition of the Phosphoethanolamine Methyltransferases of the Human Malaria Parasites Plasmodium vivax and Plasmodium knowlesi

Figure 4

PkPMT and PvPMT complement the loss of PC synthesis from ethanolamine in yeast.

A-D: represent growth curves of pem1Δpem2Δ-pYes2.1 (A) and pem1Δpem2Δ-pYES2.1-PkPMT (B), pem1Δpem2Δ-pYES2.1-PvPMT (C), or pem1Δpem2Δ-pYES2.1-PfPMT (D) strains cultured in minimal medium containing 4% galactose and 2 mM ethanolamine in the presence or absence of 100 μM choline (Cho). E and F: Analysis of the phospholipid content of pem1Δpem2Δ-pYes2.1, pem1Δpem2Δ-pYes2.1-PkPMT, pem1Δpem2Δ-pYes2.1-PvPMT and wild type-pYes2.1 strains. The yeast strains were grown in minimal medium containing 4% galactose and 2 mM ethanolamine. The lipids were extracted, separated by TLC and visualized under UV light after ANSA spray (E). Each lipid class was scrapped off from the TLC plate and quantified by measuring phosphorous (F) as described in experimental procedures. The graph is the percentage of total lipid phosphorous in each lipid fraction. The data are represented as the means ± S. E. of three independent experiments.

Back to article page