ArticleProceedings of the National Academy of Sciences of the United States of America2001
Subcellular localization of acetyl-CoA carboxylase in the apicomplexan parasite Toxoplasma gondii.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. 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 48 papers.
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Who cites it
48 citing papers in PubMed, 111 citations in OpenAlex.
- A dedicated partitioning machinery ensures faithful inheritance of the apicoplast in Toxoplasma gondii.Nature communications · 2026Article
- Integrated Proteomic Screening Reveals Heme Enzyme Depletion Induces Cyst-like Vacuole Formation inInternational journal of molecular sciences · 2026Article
- Toxoplasmosis: Epidemiological Significance, Economic Burden, and Emerging Directions in Drug Discovery and Artificial Intelligence.International journal of microbiology · 2026Review
- The Major Facilitator Superfamily Transporter HAP12 Is Critical inInternational journal of molecular sciences · 2025Article
- Malaria parasite cysteine and aspartic proteases as key drug targets for antimalarial therapy.Journal of molecular modeling · 2025Review
- The Toxoplasma micropore mediates endocytosis for selective nutrient salvage from host cell compartments.Nature communications · 2023Article
- Identification of new components of the basal pole ofFrontiers in cellular and infection microbiology · 2022Article
- Article
- Differential contribution of two organelles of endosymbiotic origin to iron-sulfur cluster synthesis and overall fitness in Toxoplasma.PLoS pathogens · 2021Article
- Succinylated Wheat Germ Agglutinin Colocalizes with the Toxoplasma gondii Cyst Wall Glycoprotein CST1.mSphere · 2020Article
- Vitamin and cofactor acquisition in apicomplexans: SynthesisThe Journal of biological chemistry · 2020Review
- Elucidating the mitochondrial proteome ofeLife · 2018Article
- Article
- Host biotin is required for liver stage development in malaria parasites.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Two essential Thioredoxins mediate apicoplast biogenesis, protein import, and gene expression in Toxoplasma gondii.PLoS pathogens · 2018Article
- Metabolic interactions betweenF1000Research · 2018Review
- A plant/fungal-type phosphoenolpyruvate carboxykinase located in the parasite mitochondrion ensures glucose-independent survival ofThe Journal of biological chemistry · 2017Article
- Novel insights into the composition and function of the Toxoplasma IMC sutures.Cellular microbiology · 2017Article
- Article
- Drugs in development for toxoplasmosis: advances, challenges, and current status.Drug design, development and therapy · 2017Review
Corrections and comments
- Erratum issued
Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Apicomplexan parasites such as Toxoplasma gondii contain a primitive plastid, the apicoplast, whose genome consists of a 35-kb circular DNA related to the plastid DNA of plants. Plants synthesize fatty acids in their plastids. The first committed step in fatty acid synthesis is catalyzed by acetyl-CoA carboxylase (ACC). This enzyme is encoded in the nucleus, synthesized in the cytosol, and transported into the plastid. In the present work, two genes encoding ACC from T. gondii were cloned and the gene structure was determined. Both ORFs encode multidomain proteins, each with an N-terminal extension, compared with the cytosolic ACCs from plants. The N-terminal extension of one isozyme, ACC1, was shown to target green fluorescent protein to the apicoplast of T. gondii. In addition, the apicoplast contains a biotinylated protein, consistent with the assertion that ACC1 is localized there. The second ACC in T. gondii appears to be cytosolic. T. gondii mitochondria also contain a biotinylated protein, probably pyruvate carboxylase. These results confirm the essential nature of the apicoplast and explain the inhibition of parasite growth in cultured cells by herbicides targeting ACC.
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