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

The Journal of Biological Chemistry
Priya RagunathanG Grüber

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-pumping activity. We then generated a heterologous F-ATP synthase model system, which demonstrated that transfer of the mycobacterial C-terminal domain to a standard F-ATP synthase α subunit suppresses ATPase activity. Single-molecule rotation assays indicated that the introduction of this Mycobacterium-specific domain decreased the angular velocity of the power-stroke after ATP binding. Solution X-ray scattering data and NMR results revealed the solution shape of Mtα and the 3D struct...Continue Reading

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Citations

Feb 24, 2018·Pathogens·Iram Khan IqbalAshwani Kumar
May 16, 2018·Proceedings of the National Academy of Sciences of the United States of America·James L MartinWayne D Frasch
Jan 27, 2019·Proceedings of the National Academy of Sciences of the United States of America·Alice Tianbu ZhangJohn E Walker
Nov 27, 2018·Biochemistry. Biokhimii︠a︡·A S Lapashina, B A Feniouk
Nov 20, 2019·Progress in Biophysics and Molecular Biology·Neelagandan KamariahGerhard Grüber
Dec 11, 2020·Nature·Valerie Mizrahi, Clifton E Barry Iii

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