Supplementary material from "A myzozoan-specific protein is an essential membrane anchoring component of the succinate dehydrogenase complex in Toxoplasma parasites"

Succinate dehydrogenase (SDH) is a protein complex that functions in the tricarboxylic acid cycle and the electron transport chain of mitochondria. In most eukaryotes, SDH is highly conserved and comprises four subunits: SdhA and SdhB form the catalytic core of the complex, while SdhC and SdhD anchor the complex in the membrane. Toxoplasma gondii is an apicomplexan parasite that infects one-third of humans worldwide. The genome of T. gondii encodes homologues of the catalytic subunits SdhA and SdhB, although the physiological role of the SDH complex in the parasite and the identity of the membrane anchoring subunits are poorly understood. Here, we show that the SDH complex contributes to optimal proliferation and O₂ consumption in the disease-causing tachyzoite stage of the T. gondii lifecycle. We characterise a small membrane-bound subunit of the SDH complex called MPODD, which is conserved amongst myzozoans, a phylogenetic grouping that incorporates apicomplexan parasites and their closest free-living relatives. We demonstrate that TgMPODD is essential for SDH activity, and plays a key role in attaching the TgSdhA and TgSdhB proteins to the membrane anchor of the complex. Our findings highlight a unique and important feature of mitochondrial energy metabolism in apicomplexan parasites and their relatives.