Results 141 to 150 of about 2,525 (167)
Regulation of Vacuolar Proton-translocating ATPase Activity and Assembly by Extracellular pH [PDF]
Journal of Biological Chemistry, 2010 Vacuolar proton-translocating ATPases (V-ATPases) are responsible for organelle acidification in all eukaryotic cells. The yeast V-ATPase, known to be regulated by reversible disassembly in response to glucose deprivation, was recently reported to be regulated by extracellular pH as well (Padilla-López, S., and Pearce, D. A. (2006) J. Biol. Chem.
Patricia M Kane
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Cloning of Entamoeba genes encoding proteolipids of putative vacuolar proton-translocating ATPases [PDF]
Infection and Immunity, 1994 Molecular cloning techniques were used to identify genes encoding the proteolipids of putative vacuolar proton-transporting ATPases (V-ATPases; EC 3.6.1.35) of Entamoeba histolytica (Ehvma3) and Entamoeba dispar. The Ehvma3 gene encoded a 177-amino-acid peptide, with an M(r) of 18,110, which showed extensive positional identities with peptides of E ...
John Samuelson
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Proton translocation driven by ATP hydrolysis in V-ATPases
FEBS Letters, 2003 The vacuolar H+-ATPases (or V-ATPases) are a family of ATP-dependent proton pumps responsible for acidification of intracellular compartments and, in certain cases, proton transport across the plasma membrane of eukaryotic cells.
Shoko Kawasaki-Nishi +2 more
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Structure and regulation of the vacuolar ATPases
Biochimica Et Biophysica Acta - Bioenergetics, 2008 The vacuolar (H+)-ATPases (V-ATPases) are ATP-dependent proton pumps responsible for both acidification of intracellular compartments and, for certain cell types, proton transport across the plasma membrane.
Ayana Hinton, Michael Forgac
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Subunit composition, biosynthesis, and assembly of the yeast vacuolar proton-translocating ATPase
Journal of Bioenergetics and Biomembranes, 1992The yeast vacuole is acidified by a vacuolar proton-translocating ATPase (H(+)-ATPase) that closely resembles the vacuolar H(+)-ATPases of other fungi, animals, and plants. The yeast enzyme is purified as a complex of eight subunits, which include both integral and peripheral membrane proteins.
Patricia M Kane +2 more
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Mouse Atp6f, the gene encoding the 23-kDa proteolipid of vacuolar proton translocating ATPase
Gene, 2001The 23-kDa proteolipid subunit of mouse vacuolar-type proton-translocating ATPase (V-ATPase) was predicted to be a hydrophobic polypeptide of 205 amino acid residues with five putative transmembrane segments. It exhibits sequence similarity to Vma16p of Saccharomyces cerevisiae and vha-4 of Caenorhabdittis elegans (83 and 84%, respectively).
Ge-Hong Sun-Wada +2 more
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Biochimica Et Biophysica Acta - Bioenergetics, 2010 Vacuolar (H+)-ATPases, also called V-ATPases, are ATP-driven proton pumps that are highly phylogenetically conserved. Early biochemical and cell biological studies have revealed many details of the molecular mechanism of proton pumping and of the ...
Sun-Kyung Lee +2 more
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Mutational Analysis of the Catalytic Subunit of the Yeast Vacuolar Proton-Translocating ATPase
Biochemistry, 1996In order to generate a set of tools for probing structure-function relationships in the catalytic subunit of the yeast vacuolar H(+)-ATPase, the gene encoding this subunit (VMA1) was randomly mutagenized. Mutant plasmids unable to complement the growth defects of yeast cells lacking an intact VMA1 gene were isolated and sequenced.
J, Liu, P M, Kane
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Identification of inhibitors of vacuolar proton-translocating ATPase pumps in yeast by high-throughput screening flow cytometry [PDF]
Analytical Biochemistry, 2010 Fluorescence intensity of the pH-sensitive carboxyfluorescein derivative 2,7-bis(2-carboxyethyl)-5(6)-carboxyfluorescein (BCECF) was monitored by high-throughput flow cytometry in living yeast cells. We measured fluorescence intensity of BCECF trapped in yeast vacuoles, acidic compartments equivalent to lysosomes where vacuolar proton-translocating ...
Rebecca M Johnson +2 more
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Protein sorting in yeast: the role of the vacuolar protontranslocating ATPase
Journal of Cell Science, 1989ABSTRACT We are investigating the physiological roles of organelle acidification in yeast by two different approaches. First, we have identified two mutants which are defective in acidification of the yeast lysosome-like vacuole from among a collection of mutants which mis-sort soluble vacuolar proteins to the cell surface. These mutants
P M, Kane +3 more
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