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Malaria parasites retain a relict plastid (apicoplast) from a photosynthetic ancestor shared with dinoflagellate algae. The apicoplast is a useful drug target; blocking housekeeping pathways such as genome replication and translation in the organelle kills parasites and protects against malaria. The apicoplast of  Plasmodium falciparum  encodes 30 proteins and a suite of rRNAs and tRNAs that facilitate their expression.  orf 105 is a hypothetical apicoplast gene that would encode a small protein ( Pf Orf105) with a predicted C-terminal transmembrane domain. We produced antisera to a predicted peptide within  Pf Orf105. Western blot analysis confirmed expression of  orf 105 and immunofluorescence localised the gene product to the apicoplast.  Pforf 105 encodes a membrane protein that has an apparent mass of 17.5 kDa and undergoes substantial turnover during the 48-hour asexual life cycle of the parasite in blood stages. The effect of actinonin, an antimalarial with a putative impact on post-translational modification of apicoplast proteins like  Pf Orf105, was examined. Unlike other drugs perturbing apicoplast housekeeping that induce delayed death, actinonin kills parasites immediately and has an identical drug exposure phenotype to the isopentenyl diphosphate synthesis blocker fosmidomycin. Open reading frames of similar size to  Pf Orf105, which also have predicted C-terminal trans membrane domains, occur in syntenic positions in all sequenced apicoplast genomes from Phylum Apicomplexa. We therefore propose to name these genes  ycf 93 (h y pothetical  c hloroplast reading  f rame 93) according to plastid gene nomenclature convention for conserved proteins of unknown function.

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Ycf93 (Orf105), a Small Apicoplast-Encoded Membrane Protein in the Relict Plastid of the Malaria Parasite Plasmodium falciparum That Is Conserved in Apicomplexa