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

  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},
Stoichiometry of Energy Coupling by Proton-Translocating ATPases: A History of Variability
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
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.
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
Comparison of the H+/ATP ratios of the H+-ATP synthases from yeast and from chloroplast
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.
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
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.


The evolution of H+-ATPases.
Evolution of the vacuolar H+-ATPase: implications for the origin of eukaryotes.
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).
The evolution of chemiosmotic energy coupling.
Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondria.
H-ATPase Activity from Storage Tissue of Beta vulgaris: II. H/ATP Stoichiometry of an Anion-Sensitive H-ATPase.
The result suggests that the H(+)-ATPase does not operate near equilibrium but is regulated by cellular factors other than energy supply.