Highly diverged novel subunit composition of apicomplexan F-type ATP synthase identified from Toxoplasma gondii

PLoS Biology
Rahul SalunkeDhanasekaran Shanmugam

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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Sep 12, 2018·ELife·Diego HuetSebastian Lourido
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Methods Mentioned

BETA
immunoprecipitation
in silico methods
transgenic
PCRs
PCR
ion exchange chromatography
size exclusion chromatography

Software Mentioned

R
Excel
Protein Lynx Global Server ( PLGS
Zen
Clustalw
Cladogram
Scer
HHPred
MPI
Custal omega

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