Results 1 to 10 of about 2,277 (122)
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 Kane
exaly +3 more sources
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
exaly +3 more sources
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.
Karlett PARRA, Samuel Lee
exaly +4 more sources
Sorting of the Yeast Vacuolar-type, Proton-translocating ATPase Enzyme Complex (V-ATPase) [PDF]
Journal of Biological Chemistry, 2012 Vacuolar proton-translocating ATPase (V-ATPase) is a central regulator of cellular pH homeostasis, and inactivation of all V-ATPase function has been shown to prevent infectivity in Candida albicans. V-ATPase subunit a of the Vo domain (Voa) is present as two fungal isoforms: Stv1p (Golgi) and Vph1p (vacuole).
Gregory C. Finnigan +5 more
+9 more sources
Frontiers in Microbiology, 2021 The vacuole of Candida albicans plays a significant role in many processes including homeostasis control, cellular trafficking, dimorphic switching, and stress tolerance.
Quanzhen Lv, Lan Yan, Yuanying Jiang
doaj +1 more source
Conformation of a Peptide Encompassing the Proton Translocation Channel of Vacuolar H+-ATPase [PDF]
Biophysical Journal, 2007 The structural properties of a crucial transmembrane helix for proton translocation in vacuolar ATPase are studied using double site-directed spin-labeling combined with electron spin resonance (ESR) (or electron paramagnetic resonance) and circular dichroism spectroscopy in sodium dodecyl sulfate micelles.
Vos, W.L., Vermeer, L.S., Hemminga, M.A.
openaire +3 more sources
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.
J J, Tomashek +4 more
openaire +2 more sources
Identification and Reconstitution of an Isoform of the 116-kDa Subunit of the Vacuolar Proton Translocating ATPase [PDF]
Journal of Biological Chemistry, 1999 We have identified a cDNA encoding an isoform of the 116-kDa subunit of the bovine vacuolar proton translocating ATPase. The predicted protein sequence of the new isoform, designated a2, consists of 854 amino acids with a calculated molecular mass of 98,010 Da; it has approximately 50% identity to the original isoform (a1) we described (Peng, S.-B ...
S B, Peng +7 more
openaire +2 more sources
Resolution of Subunit Interactions and Cytoplasmic Subcomplexes of the Yeast Vacuolar Proton-translocating ATPase [PDF]
Journal of Biological Chemistry, 1996 The vacuolar proton-translocating ATPase is the principal energization mechanism that enables the yeast vacuole to perform most of its physiological functions. We have undertaken an examination of subunit-subunit interactions and assembly states of this enzyme.
J J, Tomashek +3 more
openaire +2 more sources
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.
K J, MacLeod +3 more
openaire +2 more sources