title: Structure, molecular genetics, and evolution of vacuolar H+-ATPases.
abstract: Proton-ATPases can be divided into three classes denoted as P-, F-, and V-ATPases. The P-ATPases are evolutionarily distinct from the F- and V-type ATPases which have been shown to be related, probably evolved from a common ancestral enzyme. Like F-ATPases, V-ATPases are composed of two distinct structures: a catalytic sector that is hydrophilic in nature and a hydrophobic membrane sector which functions in proton conduction. Recent studies on the molecular biology of vacuolar H+-ATPases revealed surprising findings about the evolution of pronon pumps as well as important clues for the evolution of eukaryotic cells.
authors.affiliation: Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110.
authors.forename: N
authors.initials: N
authors.lastname: Nelson
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001419:Bacteria / Q000201:enzymology / Q000235:genetics; D005075:Biological Evolution; D002417:Cattle; D002837:Chromaffin Granules / Q000201:enzymology; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D008969:Molecular Sequence Data; D006180:Proton-Translocating ATPases / Q000235:genetics*; D012441:Saccharomyces cerevisiae / Q000201:enzymology / Q000235:genetics; D012689:Sequence Homology, Nucleic Acid; D014617:Vacuoles / Q000201:enzymology*
chemical_list: D006180:Proton-Translocating ATPases