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Submitted on September 11, 2007
Seattle Biomedical Research Institute, Seattle, WA 98109
Corresponding Author: ken.stuart{at}sbri.org
African trypanosomes, early diverged eukaryotes and the agents of sleeping sickness, have several basic cellular processes that are remarkably divergent from those in their mammalian hosts. They have large mitochondria and switch between oxidative phosphorylation and glycolysis as the major pathways for energy generation during their life cycle. We report here the identification and characterization of several multi-protein mitochondrial complexes from procyclic form Trypanosoma brucei. These were identified and purified using a panel of monoclonal antibodies that were generated against a sub-mitochondrial protein fraction and using TAP-tag affinity chromatography, and localized within the cells by immunofluorescence. Protein composition analyses by mass spectrometry revealed substantial divergence of oxidoreductase complex from other organisms, and identified a novel complex that may have function associated with nucleic acids. The relationship to divergent physiological processes in these pathogens is discussed.
Revised on December 4, 2007
Accepted on December 11, 2007
Mitochondrial complexes in trypanosoma brucei: a novel complex and a unique oxidoreductase complex
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