Evolution of proton pumping ATPases: Rooting the tree of life

  title={Evolution of proton pumping ATPases: Rooting the tree of life},
  author={Johann Peter Gogarten and Lincoln Taiz},
  journal={Photosynthesis Research},
Proton pumping ATPases are found in all groups of present day organisms. The F-ATPases of eubacteria, mitochondria and chloroplasts also function as ATP synthases, i.e., they catalyze the final step that transforms the energy available from reduction/oxidation reactions (e.g., in photosynthesis) into ATP, the usual energy currency of modern cells. The primary structure of these ATPases/ATP synthases was found to be much more conserved between different groups of bacteria than other parts of the… 

Evolutionary primacy of sodium bioenergetics

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.

Rotary Ion-Translocating ATPases/ATP Synthases: Diversity, Similarities, and Differences

This review describes the diversity of rotary ion-translocating ATPases from different organisms and compares the structural, functional, and regulatory features of these enzymes.

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.

Bioenergetics of Archaea: ATP Synthesis under Harsh Environmental Conditions

The membrane-embedded electrically-driven motor of archaea is very different in archaea with sometimes novel, exceptional subunit composition and coupling stoichiometries that may reflect the differences in energy-conserving mechanisms as well as adaptation to temperatures at or above 100°C.

Ancient origin of the vacuolar H+-ATPase 69-kilodalton catalytic subunit superfamily

Comparison of plant and fungal V-ATPase catalytic subunit gene structure indicates that introns accrued in the plant homologs following the bifurcation of plants and fungi but prior to the gene duplication event that gave rise to the vat69A and vat 69B genes approximately 45 million years ago.

Isolation of a complete A1AO ATP synthase comprising nine subunits from the hyperthermophile Methanococcus jannaschii

This is the first description of an A1AO ATPase preparation in which the two domains (A1 and AO) are fully conserved and functionally coupled.

A sodium ion‐dependent A1AO ATP synthase from the hyperthermophilic archaeon Pyrococcus furiosus

The rotor subunit c of the A1AO ATP synthase of the hyperthermophilic archaeon Pyrococcus furiosus contains a conserved Na+‐binding motif, indicating that Na+ is a coupling ion. To experimentally

Is ATP synthesized by a vacuolar-ATPase in the extremely halophilic bacteria?

The proton-dependent synthesis of ATP was demonstrated in representative members of the genera Halobacterium, Haloarcula, andHaloferax and suggest that ATP synthesis in these organisms is brought about by an F0F1-APT synthase.

A Phylogenomic Census of Molecular Functions Identifies Modern Thermophilic Archaea as the Most Ancient Form of Cellular Life

The distribution of GO terms in superkingdoms confirms that Archaea appears to be the simplest and most ancient form of cellular life, while Eukarya is the most diverse and recent.



The progenitor of ATP synthases was closely related to the current vacuolar H+‐ATPase

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).

Molecular Evolution of H+-ATPases. I. Methanococcus and Sulfolobus are Monophyletic with Respect to Eukaryotes and Eubacteria

Phylogenetic analysis using Felsenstein's maximum likelihood method and Lake's evolutionary parsimony method confirmed that the H+- ATPases of the two archaebacteria, Methanococcus and Sulfolobus, when compared to eukaryotic vacuolar-type ATPases and eubacterial F0F1-ATPases, form a monophyletic group.

The vacuolar ATPase of Neurospora crassa contains an F1-like structure.

The overall structure of the vacuolar ATPase is similar to that of F0F1-ATPases; however, the sizes of the component polypeptides and the factors that can cause dissociation are different.

Ultrastructural Comparison of the Vacuolar and Mitochondrial H+‐ATPases of Daucus carota

The V1 complexes of carrot are thus similar in form to the V1complex of Neurospora, which are believed to be organized into peripheral and integral membrane complexes.

Molecular cloning of the beta-subunit of a possible non-F0F1 type ATP synthase from the acidothermophilic archaebacterium, Sulfolobus acidocaldarius.

The distant homology of the S. acidocaldarius ATPase alpha and beta subunits when compared to those of F0F1-ATPases indicates that this archaebacterial ATPase belongs to an ion-translocating ATPase family uniquely different than F0f1- ATPases even if S. Acidocaldarian ATPase and F 0F 1-ATpases have been derived from a common ancestral ATPase.

A gene encoding the proteolipid subunit of Sulfolobus acidocaldarius ATPase complex.

Origin of the eukaryotic nucleus determined by rate-invariant analysis of rRNA sequences

Using evolutionary parsimony, a newly developed rate-invariant treeing algorithm, the eukaryotic ribosomal rRNA genes are shown to have evolved from the eocytes, a group of extremely thermophilic, sulphur-metabolizing, anucleate cells that probably lacked nuclei, metabolized sulphur and lived at near-boiling temperatures.