Elucidating the mitochondrial proteome of Toxoplasma gondii reveals the presence of a divergent cytochrome c oxidase

• Published in: eLife Vol. 7
• Main Authors: Seidi, Azadeh, Muellner-Wong, Linden S, Rajendran, Esther, Tjhin, Edwin T, Dagley, Laura F, Aw, Vincent Yt, Faou, Pierre, Webb, Andrew I, Tonkin, Christopher J, van Dooren, Giel G
• Format: Journal Article
• Language: English
• Published: England eLife Science Publications, Ltd 11.09.2018; eLife Sciences Publications Ltd; eLife Sciences Publications, Ltd
• Subjects: Amino acids; Animals; apicomplexans; Biology; Biosynthesis; Biotinylation; Computational Biology; Cytochrome; Cytochrome c; Cytochrome oxidase; Cytochrome-c oxidase; Dehydrogenases; Electron Transport Complex IV - metabolism; Enzymes; Gene Knockdown Techniques; Genes; Medical research; Microbiology and Infectious Disease; Mitochondria; Mitochondria - metabolism; Mitochondrial Membranes - metabolism; Mitochondrial Proteins - metabolism; Oxidases; Oxygen Consumption; Parasites; Parasites - growth & development; Parasites - metabolism; Phenotype; Phylogeny; Protein composition; Proteins; Proteome - metabolism; Proteomes; Proteomics; Protozoan Proteins - metabolism; Queries; Software; Sulfur; Toxoplasma; Toxoplasma - growth & development; Toxoplasma - metabolism; Toxoplasma gondii; Victoria Australia; Toxoplasma; microbiology; apicomplexans; proteomics; infectious disease; mitochondria
• ISSN: 2050-084X; 2050-084X
• DOI: 10.7554/elife.38131

The mitochondrion of apicomplexan parasites is critical for parasite survival, although the full complement of proteins that localize to this organelle has not been defined. Here we undertake two independent approaches to elucidate the mitochondrial proteome of the apicomplexan . We identify approximately 400 mitochondrial proteins, many of which lack homologs in the animals that these parasites infect, and most of which are important for parasite growth. We demonstrate that one such protein, termed ApiCox25, is an important component of the parasite cytochrome oxidase (COX) complex. We identify numerous other apicomplexan-specific components of COX, and conclude that apicomplexan COX, and apicomplexan mitochondria more generally, differ substantially in their protein composition from the hosts they infect. Our study highlights the diversity that exists in mitochondrial proteomes across the eukaryotic domain of life, and provides a foundation for defining unique aspects of mitochondrial biology in an important phylum of parasites.