Fig. 1. Schematics of GFP fusions expressed in P.falciparum. (A) Plasmodium falciparum ACP with (i) bipartite leader, and GFP fusions (ii) ACP_full–GPF and (iii) ACP_leader–GFP (s, signal peptide; t, transit peptide; shaded transition between the transit peptide and ACP indicates uncertainty of the precise boundary). (B) Signal and transit peptide deletion GFP fusions (i) ACP_transit–GFP and (ii) ACP_signal–GFP. (C) Plasmodium falciparum FabH protein with (i) bipartite leader and (ii) GFP fusion FabH_leader–GFP represented schematically and (iii) in sequence form. Mutations engineered into fusions FabH_leader[T40A]–GFP and FabH_leader[T40/49A]–GFP are indicated in (iv) and (v), respectively. N-terminal lower case sequence represents the signal peptide with the predicted cleavage point indicated (\). Upper case sequence indicates transit peptide domain and the C-terminal lower case sequence indicates the first conserved residues shared amongst FabH sequences in other organisms.