Gene duplication as a means for altering H+/ATP ratios during the evolution of Fo F1 ATPases and synthases
- 1 January 1990
- journal article
- review article
- Published by Wiley in FEBS Letters
- Vol. 259 (2), 227-229
- https://doi.org/10.1016/0014-5793(90)80014-a
Abstract
In the evolution of the FoF1 family of proton‐translocating membrane complexes, two reversals in function appear to have occurred, first changing it from an ATPase to an ATP synthase and then back again to an ATPase. Here we suggest that with each change in function, the ratio of protons transported per ATP hydrolyzed or synthesized (H+/ATP) was altered in order for the complex to better adapt to its new role. We propose that this was accomplished by gene duplication with partial loss in the number of functional catalytic sites (to increase H+/ATP) or functional proton channels (to decrease H+/ATP). This method of changing the H+/ATP ratio preserved overall structural features of the complex essential to energy coupling.This publication has 23 references indexed in Scilit:
- Evolution of the vacuolar H+-ATPase: implications for the origin of eukaryotes.Proceedings of the National Academy of Sciences, 1989
- The evolution of H+-ATPasesTrends in Biochemical Sciences, 1989
- cDNA sequence encoding the 16-kDa proteolipid of chromaffin granules implies gene duplication in the evolution of H+-ATPases.Proceedings of the National Academy of Sciences, 1988
- Subunit stoichiometry and juxtaposition of the photosynthetic coupling factor 1: Immunoelectron microscopy using monoclonal antibodiesProceedings of the National Academy of Sciences, 1985
- Primary structure and subunit stoichiometry of F1-ATPase from bovine mitochondriaJournal of Molecular Biology, 1985
- H+-ATPase Activity from Storage Tissue of Beta vulgarisPlant Physiology, 1984
- The Mr‐value of chloroplast coupling factor 1FEBS Letters, 1983
- Adenine nucleotide binding sites on beef heart F1-ATPase. Evidence for three exchangeable sites that are distinct from three noncatalytic sites.Journal of Biological Chemistry, 1982
- The proteolipid of a mutant ATPase from Escherichia coli defective in H+‐conduction contains a glycine instead of the carbodiimide‐reactive aspartyl residueFEBS Letters, 1980
- The evolution of chemiosmotic energy couplingJournal of Theoretical Biology, 1976