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In the infectious stage of  Trypanosoma brucei , an important parasite of humans and livestock, the mitochondrial (mt) membrane potential (Δψ m ) is uniquely maintained by the ATP hydrolytic activity and subsequent proton pumping of the essential F o F 1 -ATPase. Intriguingly, this multiprotein complex contains several trypanosome-specific subunits of unknown function. Here, we demonstrate that one of the largest novel subunits, ATPaseTb2, is membrane-bound and localizes with monomeric and multimeric assemblies of the FoF1-ATPase. Moreover, RNAi silencing of ATPaseTb2 quickly leads to a significant decrease of the Δψ m  that manifests as a decreased growth phenotype, indicating that the F o F 1 -ATPase is impaired. To further explore the function of this protein, we employed a trypanosoma strain that lacks mtDNA (dyskinetoplastic, Dk) and thus subunit a, an essential component of the proton pore in the membrane F o -moiety. These Dk cells generate the Δψ m  by combining the hydrolytic activity of the matrix-facing F 1 -ATPase and the electrogenic exchange of ATP 4 - for ADP 3 - by the ATP/ADP carrier (AAC). Surprisingly, in addition to the expected presence of F1-ATPase, the monomeric and multimeric F o F 1 -ATPase complexes were identified. In fact, the immunoprecipitation of a F 1 -ATPase subunit demonstrated that ATPaseTb2 was a component of these complexes. Furthermore, RNAi studies established that the membrane-bound ATPaseTb2 subunit is essential for maintaining normal growth and the Δψ m  of Dk cells. Thus, even in the absence of subunit a, a portion of the F o F 1 -ATPase is assembled in Dk cells.

ATPaseTb2, a Unique Membrane-bound FoF1-ATPase Component, Is Essential in Bloodstream and Dyskinetoplastic Trypanosomes