PT  - JOURNAL ARTICLE
AU  - Caroline E. Dewar
AU  - Silke Oeljeklaus
AU  - Bettina Warscheid
AU  - André Schneider
TI  - Characterisation of a highly diverged mitochondrial ATP synthase peripheral stalk subunit <em>b</em> in <em>Trypanosoma brucei</em>
AID  - 10.1101/2021.10.13.464200
DP  - 2021 Jan 01
TA  - bioRxiv
PG  - 2021.10.13.464200
4099  - http://biorxiv.org/content/early/2021/10/13/2021.10.13.464200.short
4100  - http://biorxiv.org/content/early/2021/10/13/2021.10.13.464200.full
AB  - The mitochondrial F1Fo ATP synthase of Trypanosoma brucei has been studied in detail. Whereas its F1 moiety is relatively highly conserved in structure and composition, the same is not the case for the Fo part and the peripheral stalk. A core subunit of the latter, the normally conserved subunit b, could not be identified in trypanosomes suggesting that it might be absent. Here we have identified a 17 kDa mitochondrial protein of the inner membrane that is essential for normal growth, efficient oxidative phosphorylation and membrane potential maintenance. Pulldown experiments and native PAGE analysis indicate that the protein is associated with the F1Fo ATP synthase. Its ablation reduces the levels of Fo subunits, but not those of F1, and disturbs the cell cycle. HHpred analysis showed that the protein has structural similarities to subunit b of other species, indicating that the Fo part of the trypanosomal ATP synthase does contain a highly diverged subunit b. Thus, the Fo part of the trypanosomal ATPase synthase may be more widely conserved than initially thought.Competing Interest StatementThe authors have declared no competing interest.