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Eukaryotic Cell, January 2006, p. 45-53, Vol. 5, No. 1
1535-9778/06/$08.00+0     doi:10.1128/EC.5.1.45-53.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

ATP Synthase Is Responsible for Maintaining Mitochondrial Membrane Potential in Bloodstream Form Trypanosoma brucei

Silvia V. Brown, Paul Hosking, Jinlei Li, and Noreen Williams*

Department of Microbiology and Immunology and Witebsky Center for Microbial Pathogenesis and Immunology, 253 Biomedical Research Building, University at Buffalo, Buffalo, New York 14214

Received 25 July 2005/ Accepted 4 November 2005

The mitochondrion of Trypanosoma brucei bloodstream form maintains a membrane potential, although it lacks cytochromes and several Krebs cycle enzymes. At this stage, the ATP synthase is present at reduced, although significant, levels. To test whether the ATP synthase at this stage is important for maintaining the mitochondrial membrane potential, we used RNA interference (RNAi) to knock down the levels of the ATP synthase by targeting the F1-ATPase {alpha} and ß subunits. RNAi-induced cells grew significantly slower than uninduced cells but were not morphologically altered. RNAi of the ß subunit decreased the mRNA and protein levels for the ß subunit, as well as the mRNA and protein levels of the {alpha} subunit. Similarly, RNAi of {alpha} subunit decreased the {alpha} subunit transcript and protein levels, as well as the ß-subunit transcript and protein levels. In contrast, {alpha} and ß RNAi knockdown resulted in a 60% increase in the F0 complex subunit 9 protein levels without a significant change in the steady-state transcript levels of this subunit. The F0-32-kDa subunit protein expression, however, remained stable throughout induction of RNAi for {alpha} or ß subunits. Oligomycin-sensitive ATP hydrolytic and synthetic activities were decreased by 43 and 44%, respectively. Significantly, the mitochondrial membrane potential of {alpha} and ß RNAi cells was decreased compared to wild-type cells, as detected by MitoTracker Red CMXRos fluorescence microscopy and flow cytometry. These results support the role of the ATP synthase in the maintenance of the mitochondrial membrane potential in bloodstream form T. brucei.

* Corresponding author. Mailing address: 253 Biomedical Research Building, Department of Microbiology, University at Buffalo, Buffalo, NY 14214. Phone: (716) 829-2279. Fax: (716) 829-2158. E-mail: nw1{at}acsu.buffalo.edu.

Eukaryotic Cell, January 2006, p. 45-53, Vol. 5, No. 1
1535-9778/06/$08.00+0     doi:10.1128/EC.5.1.45-53.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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