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National Repository of Grey Literature 2 records found  Search took 0.00 seconds. 
FoF1-ATP synthase/ATPase in the parasitic protist, \kur{Trypanosoma brucei}
 ŠUBRTOVÁ, Karolína
This thesis primarily focuses on the FoF1-ATP synthase/ATPase complex in the parasitic protist, Trypanosoma brucei. Instead of its normal aerobic function to synthesize ATP, it is required to hydrolyze ATP to maintain the m in the infective bloodstream stage of T. brucei and the related parasite, T. b. evansi. To better understand the composition, structure and function of this druggable target, my work focused on deciphering the function of three of the unique Euglenozoa specific subunits that comprise this complex molecular machine. Furthermore, the ADP/ATP carrier, which provides substrates for the FoF1-ATP synthase/ATPase, was functionally characterized and evaluated if it is physically associated with the complexes of the oxidative phosphorylation pathway.
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Interactions of Trypanosoma brucei FOF1 ATP Synthase Subunits - An Application of Yeast Two Hybrid
 GUGGENBERGER, Matthias
The FOF1 -ATP synthase has a unique composition and function in Trypanosoma brucei, a flagellated parasite endemic to developing regions of the world where it causes Human African Trypanosomiasis (HAT) and Nangana in cattle. Currently there are no good treatments to cure the disease as most of the medicine is antiquated, difficult to administer and highly toxic. Because of the unique properties of the T. brucei FOF1-ATP synthase, this enzyme is considered a possible drug target. This final component of the oxidative phosphorylation pathway actually works in reverse during the infectious stage of this parasite as it needs to hydrolyze ATP to maintain the essential mitochondrial membrane potential in the absence of a cytochrome mediated respiratory chain. In addition to the well conserved eukaryotic subunits, this large complex is also comprised of several subunits that have no known homology outside of kinetoplastids, an ancient group of protists with a unique mitochondrial DNA structure. To further explore the composition and organization of this potential drug target, we employed the technique of yeast two-hybrid to map the protein-protein interactions of the individual subunits. Our preliminary results suggest that important information about the organization of the T. brucei FOF1-ATP synthase can be gleaned from this experimental approach.
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