ArticlePLoS biology2018
Highly diverged novel subunit composition of apicomplexan F-type ATP synthase identified from Toxoplasma gondii.
Article in PLoS biology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
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- ToxoNet: A high confidence map of protein-protein interactions in Toxoplasma gondii.PLoS computational biology · 2024Article
- Mitochondrial dysfunction induced by bedaquiline as an anti-Toxoplasma alternative.Veterinary research · 2023Article
- Continuous Cropping Inhibits Photosynthesis ofPlants (Basel, Switzerland) · 2023Article
- Unique Properties of Apicomplexan Mitochondria.Annual review of microbiology · 2023Review
- The persistent homology of mitochondrial ATP synthases.iScience · 2023Article
- The mystery of massive mitochondrial complexes: the apicomplexan respiratory chain.Trends in parasitology · 2022Review
- Parasite powerhouse: A review of the Toxoplasma gondii mitochondrion.The Journal of eukaryotic microbiology · 2022Review
- Temporal and thermal profiling of theeLife · 2022Article
- Identification and Validation ofMicroorganisms · 2022Article
- Real-Time Analysis of Mitochondrial Electron Transport Chain Function inBio-protocol · 2022Article
- Redesigned and reversed: architectural and functional oddities of the trypanosomal ATP synthase.Parasitology · 2021Review
- Composition and stage dynamics of mitochondrial complexes in Plasmodium falciparum.Nature communications · 2021Article
- Supramolecular associations between atypical oxidative phosphorylation complexes of Euglena gracilis.Journal of bioenergetics and biomembranes · 2021Article
- Reevaluation of theGenome research · 2021Article
Corrections and comments
- Erratum issued
Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The mitochondrial F-type ATP synthase, a multisubunit nanomotor, is critical for maintaining cellular ATP levels. In T. gondii and other apicomplexan parasites, many subunit components necessary for proper assembly and functioning of this enzyme appear to be missing. Here, we report the identification of 20 novel subunits of T. gondii F-type ATP synthase from mass spectrometry analysis of partially purified monomeric (approximately 600 kDa) and dimeric (>1 MDa) forms of the enzyme. Despite extreme sequence diversification, key FO subunits a, b, and d can be identified from conserved structural features. Orthologs for these proteins are restricted to apicomplexan, chromerid, and dinoflagellate species. Interestingly, their absence in ciliates indicates a major diversion, with respect to subunit composition of this enzyme, within the alveolate clade. Discovery of these highly diversified novel components of the apicomplexan F-type ATP synthase complex could facilitate the development of novel antiparasitic agents. Structural and functional characterization of this unusual enzyme complex will advance our fundamental understanding of energy metabolism in apicomplexan species.
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