Article ID Journal Published Year Pages File Type
5915525 Molecular and Biochemical Parasitology 2012 4 Pages PDF
Abstract

Polyprenyl-diphosphate synthase is a key enzyme in the biosynthesis of ubiquinone, a molecule considered essential for a typical eukaryotic cell. Its orthologue in the American stercorarian flagellate Trypanosoma cruzi, solanesyl diphosphate synthase, has been previously localized into the glycosomes. We wondered whether this unique cellular localization is shared by other trypanosome species. Using digitonin permeabilization, immunofluorescence and in situ tagging techniques, we show that in Trypanosoma brucei, the African salivarian flagellate, the enzyme localizes to the mitochondrion.

Graphical abstractDownload high-res image (117KB)Download full-size imageHighlight► Coq1p orthologue in Trypanosoma brucei, solanesyl-diphosphate synthase (TbSPPS), had been identified. ► Digitonin permeabilization releases TbSPPS together with the mitochondrial RNA-binding protein (MRP1) ► The C-terminally tagged TbSPPS displayed (immuno)fluorescence exclusively in the mitochondrion.

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