Highly diverged novel subunit composition of apicomplexan F-type ATP synthase identified from Toxoplasma gondii
KAUST DepartmentBiological and Environmental Sciences and Engineering (BESE) Division
Pathogen Genomics Laboratory
Permanent link to this recordhttp://hdl.handle.net/10754/627933
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AbstractThe 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.
CitationSalunke R, Mourier T, Banerjee M, Pain A, Shanmugam D (2018) Highly diverged novel subunit composition of apicomplexan F-type ATP synthase identified from Toxoplasma gondii. PLOS Biology 16: e2006128. Available: http://dx.doi.org/10.1371/journal.pbio.2006128.
SponsorsScience & Engineering Research Board (SERB), India http://www.serb.gov.in (grant number EMR/2016/003588). DS and MB are supported by this funding. The funder had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. King Abdullah University of Science and Technology (KAUST) Office of Sponsored Research (OSR) https://osr.kaust.edu.sa (grant number OCRF-2014-CRG3-2267 and BAS/1/1020-01-01). TM and AP are supported by this funding. The funder had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript. Council of Scientific and Industrial Research, India. http://csirhrdg.res.in/ (grant number). RS was awarded CSIR PhD Fellowship. The funder had no role in study design, data collection and analysis, decision to publish, or preparation of the manuscript.
PublisherCold Spring Harbor Laboratory
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