Assembly of the Escherichia coli FoF1 ATP synthase involves distinct subcomplex formation.

@article{DeckersHebestreit2013AssemblyOT,
  title={Assembly of the Escherichia coli FoF1 ATP synthase involves distinct subcomplex formation.},
  author={Gabriele Deckers-Hebestreit},
  journal={Biochemical Society transactions},
  year={2013},
  volume={41 5},
  pages={1288-93}
}
The ATP synthase (FoF1) of Escherichia coli couples the translocation of protons across the cytoplasmic membrane by Fo to ATP synthesis or hydrolysis in F1. Whereas good knowledge of the nanostructure and the rotary mechanism of the ATP synthase is at hand, the assembly pathway of the 22 polypeptide chains present in a stoichiometry of ab2c10α3β3γδϵ has so far not received sufficient attention. In our studies, mutants that synthesize different sets of FoF1 subunits allowed the characterization… CONTINUE READING

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Functional production of the Na+ F1Fo ATP synthase from Acetobacterium woodii in Escherichia coli requires the native AtpI

G. Deckers-Hebestreit, V. Müller
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