Evolution of structure and function of V-ATPases

Abstract

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 shows that the V- and F-type ATPases evolved from the same enzyme already present in the last common ancestor of all known extant life forms. The catalytic and noncatalytic subunits found in the dissociable head groups of the V/F-type ATPases are paralogous subunits, i.e., these two types of subunits evolved from a common ancestral gene. The gene duplication giving rise to these two genes (i.e., encoding the catalytic and noncatalytic subunits) predates the time of the last common ancestor. Mapping of gene duplication events that occurred in the evolution of the proteolipid, the noncatalytic and the catalytic subunits, onto the tree of life leads to a prediction for the likely subunit structure of the encoded ATPases. A correlation between structure and function of V/F-ATPases has been established for present-day organisms. Implications resulting from this correlation for the bioenergetics operative in proto-eukaryotes and in the last common ancestor are presented. The similarities of the V/F-ATPase subunits to an ATPase-like protein that was implicated to play a role in flagellar assembly are evaluated. Different V-ATPase isoforms have been detected in some higher eukaryotes. These data are analyzed with respect to the possible function of the different isoforms (tissue specific, organelle specific) and with respect to the point in their evolution when these gene duplications giving rise to the isoforms had occurred, i.e., how far these isoforms are distributed.

The vacuolar H+-ATPase: a universal proton pump of eukaryotes

“…Inhibition of V-ATPase activity by nitrate has been widely documented in a variety of systems [25,29,31,36,46,[164][165][166][167], and appears to occur as the sum effect of two distinct phenomena [165,166]. At high concentrations, nitrate may act as a chaotropic agent, with inhibition resulting from the dissociation of peripheral V " subunits from the membrane [25,31,36,165].…”

Molecular Cloning and Expression of Three Isoforms of the 100-kDa a Subunit of the Mouse Vacuolar Proton-translocating ATPase

“…V-ATPases are present in a variety of intracellular compartments, including clathrin-coated vesicles, endosomes, lysosomes, Golgi-derived vesicles, chromaffin granules, synaptic vesicles, and the central vacuoles of yeast, Neurospora, and plants (1)(2)(3)(4)(5)(6)(7)(8)(9). Vacuolar acidification is essential for such processes as receptor-mediated endocytosis, intracellular targeting, protein processing and degradation, and coupled transport.…”

“…The V-ATPases of animals, plants, and fungi are structurally very similar and are composed of two functional domains (1)(2)(3)(4)(5)(6)(7)(8)(9). The V 1 domain is a peripheral complex (molecular mass, 600 -650 kDa) composed of eight different subunits ranging in molecular mass from 70 to 14 kDa (subunits A-H) that is responsible for ATP hydrolysis.…”

The Vacuolar H+-ATPase of Clathrin-coated Vesicles Is Reversibly Inhibited by S-Nitrosoglutathione

“…The vacuolar H ϩ -ATPases (or V-ATPases 1 ) are a family of ATP-dependent proton pumps responsible for acidification of intracellular compartments in eukaryotic cells (1)(2)(3)(4)(5)(6)(7)(8). V-ATPases play an important role in such processes as receptormediated endocytosis, intracellular membrane traffic, protein processing and degradation, and coupled transport.…”