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}
}
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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.
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References

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TLDR
It is reported that the same vacuolar H-ATPase subunits are approximately equal to 50% identical to the alpha and beta subunits, respectively, of the sulfur-metabolizing Sulfolobus acidocaldarius, an archaebacterium (Archaeobacterium).
cDNA sequence encoding the 16-kDa proteolipid of chromaffin granules implies gene duplication in the evolution of H+-ATPases.
TLDR
The cloned and sequenced the gene encoding the DCCD-binding protein (proteolipid) of the H+-ATPase of bovine chromaffin granules and suggest that the proteolipids of the vacuolar H+.ATPases were evolved in parallel with the eubacterial proteolIPid, from a common ancestral gene that underwent gene duplication.
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