Sulfhydryl oxidase Erv1 is a ubiquitous and conserved protein of the mitochondrial intermembrane space that plays a role in the transport of small sulfur-containing proteins. In higher eukaryotes, Erv1 interacts with the mitochondrial import protein Mia40. However, Trypanosoma brucei lacks an obvious Mia40 homologue in its genome. Here we show by tandem affinity purification and mass spectrometry that in this excavate protist, Erv1 functions without a Mia40 homologue and most likely any other interaction partner. Down-regulation of TbErv1 caused a reduction of the mitochondrial membrane potential already within 24h to less than 50% when compared with control cells. The depletion of TbErv1 was accompanied by accumulation of trCOIV precursor, with a concomitant reduction of aconitase activity both in the cytosol and mitochondrion. Overall, TbErv1 seems to have a role in the mitochondrial translocation and Fe-S cluster assembly in the organelle.

Faculty of Sciences University of South Bohemia 37005 České Budějovice Czech Republic

Institute of Parasitology Biology Centre 37005 České Budějovice Czech Republic

Institute of Parasitology Biology Centre 37005 České Budějovice Czech Republic; Canadian Institute for Advanced Research Toronto Ontario M5G 1Z8 Canada

Citace poskytuje Crossref.org

Fe-S cluster assembly in the supergroup Excavata