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
TLDR
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.
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Proton pumping ATPases/ATPsynthases are found in all groups of present-day organisms. The structure of V- and F-type ATPases/ATP synthases is very conserved throughout evolution. Sequence analysis
The F0F1-type ATP synthases of bacteria: structure and function of the F0 complex.
TLDR
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.
  • N. Nelson
  • Biology
    Biochimica et biophysica acta
  • 1992
Evolution of proton pumping ATPases: Rooting the tree of life
TLDR
A correlation between structure and function of ATPases has been established and the location of the last common ancestor of the major domains of living organisms (archaebacteria, eubacteria and eukaryotes) can be located in the tree of life without assuming constant or equal rates of change in the different branches.
Comparison of the H+/ATP ratios of the H+-ATP synthases from yeast and from chloroplast
TLDR
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.
Evolutionary primacy of sodium bioenergetics
TLDR
Barring convergent emergence of the same set of ligands in several lineages, these findings indicate that the use of sodium gradient for ATP synthesis is the ancestral modality of membrane bioenergetics.
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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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