Results 11 to 20 of about 2,250 (114)

Vacuolar proton-translocating ATPase is required for antifungal resistance and virulence of Candida glabrata

PLOS ONE, 2019
Vacuolar proton-translocating ATPase (V-ATPase) is located in fungal vacuolar membranes. It is involved in multiple cellular processes, including the maintenance of intracellular ion homeostasis by maintaining acidic pH within the cell. The importance of V-ATPase in virulence has been demonstrated in several pathogenic fungi, including Candida albicans.
Asuka Minematsu, Taiga Miyazaki, Shintaro Shimamura, Hiroshi Nishikawa, Hironobu Nakayama, Takahiro Takazono, Tomomi Saijo, Kazuko Yamamoto, Yoshifumi Imamura, Katsunori Yanagihara, Shigeru Kohno, Hiroshi Mukae, Koichi Izumikawa   +12 more
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Sorting of the Yeast Vacuolar-type, Proton-translocating ATPase Enzyme Complex (V-ATPase) [PDF]

Journal of Biological Chemistry, 2012
Subunit a of the yeast vacuolar-type, proton-translocating ATPase enzyme complex (V-ATPase) is responsible for both proton translocation and subcellular localization of this highly conserved molecular machine. Inclusion of the Vph1p isoform causes the V-ATPase complex to traffic to the vacuolar membrane, whereas incorporation of Stv1p causes continued ...
Gregory C. Finnigan, Glen E. Cronan, Hae J. Park, Sankaranarayanan Srinivasan, Florante A. Quiocho, Tom H. Stevens   +5 more
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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 ...
S Descoteaux, Yi Yu, John Samuelson
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Mutational Analysis of the Nucleotide Binding Sites of the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1998
To further define the structure of the nucleotide binding sites on the vacuolar proton-translocating ATPase (V-ATPase), the role of aromatic residues at the catalytic sites was probed using site-directed mutagenesis of the VMA1 gene that encodes the A subunit in yeast.
Kathryn J. MacLeod, Elena Vasilyeva, James Baleja, Michael Forgac   +3 more
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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.
Theodore T. Diakov, Patricia M. Kane
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Reconstitution in Vitro of the V1 Complex from the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1997
Oligomeric assembly is a fundamental aspect of many complex enzymes. Using our native gel technique for examining subcomplexes of the V-ATPase V1 sector, we have developed an in vitro reconstitution assay for assembly of this complex. Assembly of complex II, the soluble V1 complex observed in native gels, is dependent upon the presence of divalent ...
John J. Tomashek, Brian S. Garrison, Daniel J. Klionsky   +2 more
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Transmembrane Topography of the 100-kDa a Subunit (Vph1p) of the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1999
The membrane topography of the yeast vacuolar proton-translocating ATPase a subunit (Vph1p) has been investigated using cysteine-scanning mutagenesis. A Cys-less form of Vph1p lacking the seven endogenous cysteines was constructed and shown to have 80% of wild type activity.
Xing-Hong Leng, Tsuyoshi Nishi, Michael Forgac   +2 more
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Advances in targeting the vacuolar proton-translocating ATPase (V-ATPase) for anti-fungal therapy [PDF]

Frontiers in Pharmacology, 2014
Vacuolar proton-translocating ATPase (V-ATPase) is a membrane-bound, multi-subunit enzyme that uses the energy of ATP hydrolysis to pump protons across membranes. V-ATPase activity is critical for pH homeostasis and organelle acidification as well as for generation of the membrane potential that drives secondary transporters and cellular metabolism.
Summer R. Hayek, Samuel A. Lee, Karlett J. Parra   +2 more
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V1-situated Stalk Subunits of the Yeast Vacuolar Proton-translocating ATPase [PDF]

Journal of Biological Chemistry, 1997
The proton-translocating ATPase of the yeast vacuole is an enzyme complex consisting of a large peripheral membrane sector (V1) and an integral membrane sector (V0), each composed of multiple subunits. The V1 sector contains subunits that hydrolyze ATP, whereas the V0 sector contains subunits that translocate protons across the membrane.
John J. Tomashek, Laurie A. Graham, Maria U. Hutchins, Tom H. Stevens, Daniel J. Klionsky   +4 more
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Loss of Vacuolar Proton-translocating ATPase Activity in Yeast Results in Chronic Oxidative Stress [PDF]

Journal of Biological Chemistry, 2007
Yeast mutants lacking vacuolar proton-translocating ATPase (V-ATPase) subunits (vma mutants) were sensitive to several different oxidants in a recent genomic screen (Thorpe, G. W., Fong, C. S., Alic, N., Higgins, V. J., and Dawes, I. W. (2004) Proc. Natl. Acad. Sci. U. S. A. 101, 6564-6569). We confirmed that mutants lacking a V(1) subunit (vma2Delta),
Elena Milgröm, Heba I. Diab, Frank A. Middleton, Patricia M. Kane   +3 more
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