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and kinetoplastids like Trypanosoma brucei lack canonical stator subunits but possess phylum-specific proteins that likely perform that function ( Šubrtová et al., 2015 van Lis et al., 2007).Īpicomplexans comprise a large phylum of obligate intracellular eukaryotic parasites that infect animals and cause significant human mortality and morbidity. Similarly, the ATP synthases of algae like Chlamydomonas reinhardtii and Polytomella spp. Proteomic and biochemical studies have identified several potential stator subunits in Tetrahymena thermophila and Euglena gracilis, although none appear conserved among protists ( Balabaskaran Nina et al., 2010 Perez et al., 2014). In contrast, recent studies in different protozoan species have reported unique structural and functional features in their ATP synthases. In these two species, the architecture of the ATP synthase is virtually identical, and sequence analysis and proteomics have identified homology for nearly all of the subunits that constitute the mitochondrial ATP synthase ( Wittig and Schägger, 2008). The composition of the mitochondrial ATP synthase has mainly been determined from detailed studies of purified Saccharomyces cerevisiae and Bos taurus mitochondria, both members of the eukaryotic clade Opisthokonta.
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It is therefore surprising that despite general conservation of the central subunits, the lateral elements of protozoan ATP synthases are structurally diverse, and these organisms appear to lack homologs for the stator subunits of yeast and mammals ( Lapaille et al., 2010). The stator, also known as the lateral stalk, is an essential component of the ATP synthase because it counteracts the rotation of the α and β subunits, enabling ATP synthesis ( Dickson et al., 2006). This rotation causes the conformational changes in the α and β subunits of F 1 that mediate catalysis of ATP from ADP and inorganic phosphate (P i) ( Jonckheere et al., 2012). Within their mitochondria, the proton gradient generated by the electron transport chain (ETC) drives the rotation of a ring of c subunits in F o and of the attached central stalk within F 1. The mechanism of this molecular motor is best understood for the mitochondrial ATP synthases of yeast and mammals. The complex consists of two functionally distinct portions: the hydrophilic F 1 and the membrane-bound F o ( Walker, 2013). The ATP synthase is a highly conserved protein complex found in the plasma membrane of bacteria, the inner membrane of mitochondria, and the thylakoid membrane of chloroplasts. Our findings highlight divergent features of the central metabolic machinery in apicomplexans, which may reveal new therapeutic opportunities. Depletion of ICAP2 leads to aberrant mitochondrial morphology, decreased oxygen consumption, and disassembly of the complex, consistent with its role as an essential component of the Toxoplasma ATP synthase. Our analysis shows that both proteins form part of the ATP synthase complex. Modeling suggests that two of them, ICAP2 and ICAP18, are distantly related to mammalian stator subunits. Here, we identify 11 previously unknown subunits from the Toxoplasma ATP synthase, which lack homologs outside the phylum. However, sequence-based searches fail to identify genes encoding stator subunits in apicomplexan parasites like Toxoplasma gondii or the related organisms that cause malaria. Proper ATP synthase function requires a stator linking the catalytic and rotary portions of the complex. The mitochondrial ATP synthase is a macromolecular motor that uses the proton gradient to generate ATP.