Structural conservation and functional diversity of V-ATPases.
The vacuolar system of eukaryotic cells contains a large number of organelles that are primary energized by an H(+)-ATPase that was named V-ATPase. The structure and function of V-ATPases from various sources was extensively studied in the last few years. Several genes encoding subunits of the enzyme were cloned and sequenced. The sequence information revealed the relations between V-ATPases and F-ATPases that evolved from common ancestral genes. The two families of proton pumps share structural and functional similarity. They contain distinct peripheral catalytic sectors and hydrophobic membrane sectors. Genes encoding subunits of V-ATPase in yeast cells were interrupted to yield mutants that are devoid of the enzyme and are sensitive to pH and calcium concentrations in the medium. The mutants were used to study structure, function, molecular biology, and biogenesis of the V-ATPase. They also shed light on the functional assembly of the enzyme in the vacuolar system.
Nelson
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Roche Institute of Molecular Biology, Roche Research Center, Nutley, New Jersey 07110.
D000595:Amino Acid Sequence; D005057:Eukaryotic Cells / Q000201:enzymology; D008969:Molecular Sequence Data; D017494:Proton Pumps / Q000502:physiology; D006180:Proton-Translocating ATPases / Q000737:chemistry / Q000502:physiology*; D014617:Vacuoles / Q000201:enzymology*
D017494:Proton Pumps; D006180:Proton-Translocating ATPases