Evolution of the Inhibitory and Non-Inhibitory ε, ζ, and IF₁ Subunits of the F₁F_O-ATPase as Related to the Endosymbiotic Origin of Mitochondria.

ABSTRACT: The F1FO-ATP synthase nanomotor synthesizes >90% of the cellular ATP of almost all living beings by rotating in the “forward” direction, but it can also consume the same ATP pools by rotating in “reverse.” To prevent futile F1FO-ATPase activity, several different inhibitory proteins or domains in bacteria (ε and ζ subunits), mitochondria (IF1), and chloroplasts (ε and γ disulfide) emerged to block the F1FO-ATPase activity selectively. In this study, we analyze how these F1FO-ATPase inhibitory proteins have evolved. The phylogeny of the α-proteobacterial ε showed that it diverged in its C-terminal side, thus losing both the inhibitory function and the ATP-binding/sensor motif that controls this inhibition. The losses of inhibitory function and the ATP-binding site correlate with an evolutio

SUBMITTER: Mendoza-Hoffmann F 

PROVIDER: S-EPMC9317440 | biostudies-literature | 2022 Jul

REPOSITORIES: biostudies-literature