Affinage · Plasmodium

ATPTG15

PF3D7_0825400 · ATP synthase-associated protein, putative

Audit flag: identity unverified
Annotated
2026-09-08
5 papers in source corpus 2 papers cited in narrative 2 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

PF3D7_0825400 (ATPTG15) is a putative ATP synthase-associated subunit of the Plasmodium falciparum mitochondrion. It was localized to the parasite mitochondrion as one of seven epitope-tagged canonical ATP synthase subunits, and blue native gel electrophoresis of mitochondrial membranes established that the ATP synthase complex it belongs to exceeds 1 MDa, consistent with a dimeric assembly and implying subunits beyond the canonical set (PMID:21984828). Beyond its membership in this large mitochondrial ATP synthase complex, no subunit-specific enzymatic activity, interaction, or functional role has been experimentally established for PF3D7_0825400 in the available corpus.

Mechanistic history

Synthesis pass · year-by-year structured walk · 1 step
  1. 2011 Medium

    It was unknown whether the canonical ATP synthase subunits of P. falciparum, including the product of PF3D7_0825400, are mitochondrial and assemble into a defined complex; epitope-tagging placed the protein in the mitochondrion and native gels showed it belongs to a >1 MDa dimeric complex, establishing its physical context.

    Evidence Epitope-tagging with immunofluorescence localization and blue native gel electrophoresis of mitochondrial membrane fractions in transgenic P. falciparum

    PMID:21984828

    Open questions at the time
    • No subunit-specific function or enzymatic contribution of PF3D7_0825400 was dissected; it was studied only collectively among seven subunits
    • Direct interaction partners within the complex were not resolved
    • Whether PF3D7_0825400 is required for complex assembly or activity was not tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • The specific molecular role of PF3D7_0825400 within the divergent Plasmodium ATP synthase complex — its enzymatic contribution, its direct partner subunits, and its requirement for complex assembly or activity — remains uncharacterized in the available corpus.
  • No subunit-specific interaction data
  • No structural placement within the complex
  • No genetic knockout or knockdown phenotype for PF3D7_0825400 itself

Mechanism profile

Synthesis pass · controlled-vocabulary classification
Complex memberships
Mitochondrial ATP synthase complex (>1 MDa, dimeric) [#0]

Evidence

Reading pass · 2 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2011 Seven epitope-tagged canonical ATP synthase subunits of P. falciparum, including the subunit encoded by PF3D7_0825400, were localized to the mitochondrion by immunological tools; blue native gel electrophoresis of mitochondrial membranes showed the ATP synthase complex exceeds 1 million daltons, consistent with dimeric assembly, suggesting the presence of previously unknown subunits beyond the canonical ones. Epitope-tagging and immunofluorescence localization; blue native gel electrophoresis of mitochondrial membrane fractions The Journal of biological chemistry Medium 21984828
2009 Bioinformatic and proteomics-based analysis identified candidate ATP synthase subunit a and subunit b in Plasmodium spp.; the transmembrane helix IV of ATP synthase subunit a (relevant to the F(o) sector) was found to lack an essential Arg residue present in canonical orthologs, indicating divergence of Plasmodium ATP synthase membrane anchor subunits. Computational identification using structural fingerprints and proteomics data from other protists Mitochondrion Low 19682605

Source papers

Stage 0 corpus · 5 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2015 Mitochondrial ATP synthase is dispensable in blood-stage Plasmodium berghei rodent malaria but essential in the mosquito phase. Proceedings of the National Academy of Sciences of the United States of America 91 25831536
2004 The multiple roles of the mitochondrion of the malarial parasite. Parasitology 66 15552397
2015 Triaminopyrimidine is a fast-killing and long-acting antimalarial clinical candidate. Nature communications 59 25823686
2011 ATP synthase complex of Plasmodium falciparum: dimeric assembly in mitochondrial membranes and resistance to genetic disruption. The Journal of biological chemistry 54 21984828
2009 Identification of mitochondrial Complex II subunits SDH3 and SDH4 and ATP synthase subunits a and b in Plasmodium spp. Mitochondrion 27 19682605