Stoichiometry and deletion analyses of subunits in the heterotrimeric F-ATP 
synthase c ring from the acetogenic bacterium Acetobacterium woodii

Brandt, Karsten; Müller, Daniel B.; Hoffmann, Jan; Langer, Julian David; Brutschy, Bernd; Morgner, Nina; Müller, Volker

doi:doi:10.1111/febs.13606

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Stoichiometry and deletion analyses of subunits in the heterotrimeric F-ATP synthase c ring from the acetogenic bacterium Acetobacterium woodii

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Langer, Julian David
Department of Molecular Membrane Biology, Max Planck Institute of Biophysics, Max Planck Society;

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Citation

Brandt, K., Müller, D. B., Hoffmann, J., Langer, J. D., Brutschy, B., Morgner, N., et al. (2016). Stoichiometry and deletion analyses of subunits in the heterotrimeric F-ATP synthase c ring from the acetogenic bacterium Acetobacterium woodii. The FEBS Journal, 283(3), 510-520. doi: doi:10.1111/febs.13606.

Cite as: https://hdl.handle.net/11858/00-001M-0000-002D-1D35-4

Abstract

The ion-translocating c ring of the Na⁺ F₁F_o ATP synthase of the anaerobic bacterium Acetobacterium woodii is the first heteromeric c ring found in nature that contains one V- (c₁) and two F-type-like c subunits (c₂/c₃), the latter of identical amino acid sequence. To address whether they are of equal or different importance for function, they were deleted in combination or individually. Deletion of c₁ was compensated by incorporation of two c₂/c₃ subunits but the enzyme was unstable and largely impaired in Na⁺ transport. Deletion of c₂ was compensated by incorporation of c₃ but also led to a reduction of Na⁺ transport. Deletion of c₃ had no effect. In contrast, deletion of both c₂ and c₃ led to a complete loss of ATPase activity at the cytoplasmic membrane. Mass spectrometric analysis of c₂+1 Ala and c₂+2 Ala variants revealed a copy number of 8 : 1 for c₂/c₃ which is consistent with the biochemical characteristics of the variants. These data indicate a role of c₁ in assembly and a function of c₂ as the predominant c ring constituent.