Fig. 2. Migration profiles of proteins associated with previously described complexes.

Common eukaryotic and parasite-specific protein complexes identified in mitochondrially enriched fractions of P. falciparum. a Putative EMC components, representative heatmap from sample ABS3D. All detected EMC components comigrate at an M_r^app. of ~530 kDa. b Proteasome components, representative heatmap from sample ABS3D. 20S components comigrate at an M_r^app. of ~690 kDa and to a lesser degree at ~880 kDa. 19S regulatory components comigrate at two distinct sizes, a major proportion at ~1600 kDa and a smaller fraction at ~600 kDa. c RhopH complex, representative heatmap from sample ABS1Da. PF3D7_0220200 (RhopHA1) shared RhopH complex pattern consistently and thus was putatively assigned to the RhopH complex. d LAP complex, representative heatmap from sample GCT1Da. LAP complex components in gametocytes migrated as two distinct subcomplex consisting of LAP1-3 (~460 kDa) and LAP4-5 (~310 kDa), respectively. In addition, a faint putative assembly intermediate consisting of LAP2 and LAP3 was observed at ~310 kDa. e PTEX, representative heatmap (upper panel) and line chart of iBAQ values in the 750–4000 kDa mass range from sample ABS1Da. The PTEX complex including auxiliary subunits can be observed to comigrate at an M_r^app. of ~2.8 MDa. Due to the high proportion of EXP2 present as the homooligomeric EXP2 complex at ~565 kDa, membership is only evident when comparing absolute intensity values (lower panel) instead of normalized abundances (heatmap). PTEX88 and TRX2 have much lower intensities in this mass range than core components. SG stacking gel. Corresponding Gene IDs can be found in Supplementary Data 1.