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Characterization of a highly diverged mitochondrial ATP synthase Fo subunit in Trypanosoma brucei.


ABSTRACT: The mitochondrial F1Fo ATP synthase of the parasite Trypanosoma brucei has been previously studied in detail. This unusual enzyme switches direction in functionality during the life cycle of the parasite, acting as an ATP synthase in the insect stages, and as an ATPase to generate mitochondrial membrane potential in the mammalian bloodstream stages. Whereas the trypanosome F1 moiety is relatively highly conserved in structure and composition, the Fo subcomplex and the peripheral stalk have been shown to be more variable. Interestingly, a core subunit of the latter, the normally conserved subunit b, has been resistant to identification by sequence alignment or biochemical methods. Here, we identified a 17 kDa mitochondrial protein of the inner mem

SUBMITTER: Dewar CE 

PROVIDER: S-EPMC9034290 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature