Gene duplication as a means for altering H+/ATP ratios during the evolution of Fo F1 ATPases and synthases

@article{Cross1990GeneDA,
  title={Gene duplication as a means for altering H+/ATP ratios during the evolution of Fo F1 ATPases and synthases},
  author={Richard L. Cross and Lincoln Taiz},
  journal={FEBS Letters},
  year={1990},
  volume={259}
}
Stoichiometry of Energy Coupling by Proton-Translocating ATPases: A History of Variability
TLDR
Recent discoveries concerning the structure of the ATPases, their assembly and the stoichiometry of their numerous subunits, particularly the proton-carrying proteolipid (subunit c) of the FO and V0 sectors, have shed new light on this question and raise the possibility of variable coupling ratios modulated by variable proteolIPid stoichiometries.
ATP synthases: structure, function and evolution of unique energy converters
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Recent studies on the molecular biology of the AO/FO/VO domains revealed surprising findings about duplicated and triplicated versions of the proteolipid subunit and shed new light on the evolution of these ion pumps.
The F0F1-type ATP synthases of bacteria: structure and function of the F0 complex.
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Membrane-bound ATP synthases of bacteria serve two important physiological functions: the enzyme catalyzes the synthesis of ATP from ADP and inorganic phosphate utilizing the energy of an electrochemical ion gradient and generating a transmembrane ion gradient at the expense of ATP hydrolysis.
Evolution of organellar proton-ATPases.
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Comparison of the H+/ATP ratios of the H+-ATP synthases from yeast and from chloroplast
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The data show that the thermodynamic H+/ATP ratio depends on the stoichiometry of the c-subunit, although it is not identical to the c/β ratio.
Genetic fusions of subunit c in the F0 sector of H+-transporting ATP synthase. Functional dimers and trimers and determination of stoichiometry by cross-linking analysis.
TLDR
The results show that there are 12 copies of subunit c per F0 in E. coli, the exact number having both mechanistic and structural significance.
Evolution and isoforms of V-ATPase subunits.
The structure of V- and F-ATPases/ATP synthases is remarkably conserved throughout evolution. Sequence analyses show that the V- and F-ATPases evolved from the same enzyme that was already present in
Vacuolar H+-ATPase
Arg-735 of the 100-kDa subunit a of the yeast V-ATPase is essential for proton translocation
TLDR
It is suggested that Arg-735 is absolutely required for proton transport by the V-ATPases and is discussed in the context of a revised model of the topology of the 100-kDa subunit a.
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