The uniqueness of subunit α of mycobacterial F-ATP synthases: An evolutionary variant for niche adaptation.

ABSTRACT: The F₁F₀ -ATP (F-ATP) synthase is essential for growth of Mycobacterium tuberculosis, the causative agent of tuberculosis (TB). In addition to their synthase function most F-ATP synthases possess an ATP-hydrolase activity, which is coupled to proton-pumping activity. However, the mycobacterial enzyme lacks this reverse activity, but the reason for this deficiency is unclear. Here, we report that a Mycobacterium-specific, 36-amino acid long C-terminal domain in the nucleotide-binding subunit α (Mtα) of F-ATP synthase suppresses its ATPase activity and determined the mechanism of suppression. First, we employed vesicles to show that in intact membrane-embedded mycobacterial F-ATP synthases deletion of the C-terminal domain enabled ATPase and proton-

SUBMITTER: Ragunathan P 

PROVIDER: S-EPMC5500794 | biostudies-literature | 2017 Jul

REPOSITORIES: biostudies-literature