Search results for "ATPASE"

showing 10 items of 196 documents

Absence of malolactic activity is a characteristic of H+-ATPase-deficient mutants of the lactic acid bacterium Oenococcus oeni.

2003

ABSTRACT The lack of malolactic activity in H + -ATPase-deficient mutants of Oenococcus oeni selected previously was analyzed at the molecular level. Western blot experiments revealed a spot at 60 kDa corresponding to the malolactic enzyme only in the parental strain. Moreover, the mleA transcript encoding the malolactic enzyme was not detected by reverse transcription (RT)-PCR analysis of mutants. These results suggest that the malolactic operon was not transcribed in ATPase-deficient mutants. The mleR gene encoding a LysR-type regulatory protein which should be involved in expression of the malolactic genes was described previously for O. oeni . Results obtained in this study show that th…

Transcription GeneticOperonMutantImmunoblottingMalatesApplied Microbiology and Biotechnologychemistry.chemical_compoundMalate DehydrogenaseMalolactic fermentationLactic AcidGeneOenococcus oeniEcologybiologyReverse Transcriptase Polymerase Chain ReactionLactococcus lactisGene Expression Regulation Bacterialbiology.organism_classificationPhysiology and BiotechnologyMolecular biologyLactic acidGram-Positive CocciLactococcus lactisProton-Translocating ATPaseschemistryBiochemistryLeuconostoc mesenteroidesMutationGene DeletionLeuconostocFood ScienceBiotechnologyApplied and environmental microbiology
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Regulation of stress response in Oenococcus oeni as a function of environmental changes and growth phase

2000

International audience; Oenococcus oeni is a lactic acid bacterium which is able to grow in wine and perform malolactic fermentation. To survive and grow in such a harsh environment as wine, O. oeni uses several mechanisms of resistance including stress protein synthesis. The molecular characterisation of three stress genes hsp18, clpX, trxA encoding for a small heat shock protein, an ATPase regulation component of ClpP protease and a thioredoxin, respectively, allow us to suggest the existence in O. oeni of multiple regulation mechanisms as is the case in Bacillus subtilis. One common feature of these genes is that they are expressed under the control of housekeeping promoters. The express…

Transcription Geneticmedicine.medical_treatment[SDV]Life Sciences [q-bio]bactérie lactiqueBacillus subtilisatpaseMicrobiologygène clppoenococcus oenicaractérisation moléculaire03 medical and health sciencesBacterial ProteinsHeat shock proteinOenococcus;Malolactic fermentation;Stress gene;ATPaseMalolactic fermentationmedicineprotéine de choc thermiquePromoter Regions GeneticGeneHeat-Shock ProteinsOenococcus030304 developmental biologyOenococcus oeniAdenosine Triphosphatases0303 health sciencesProteasebiology030306 microbiologyMalolactic fermentationStress genefood and beveragesGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationGram-Positive CocciBiochemistryThioredoxinOenococcusLeuconostocFood Scienceexpression des gènes
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Acidic Environment Leads to ROS-Induced MAPK Signaling in Cancer Cells

2011

Tumor micromilieu often shows pronounced acidosis forcing cells to adapt their phenotype towards enhanced tumorigenesis induced by altered cellular signalling and transcriptional regulation. In the presents study mechanisms and potential consequences of the crosstalk between extra- and intracellular pH (pH(e), pH(i)) and mitogen-activated-protein-kinases (ERK1/2, p38) was analyzed. Data were obtained mainly in AT1 R-3327 prostate carcinoma cells, but the principle importance was confirmed in 5 other cell types. Extracellular acidosis leads to a rapid and sustained decrease of pH(i) in parallel to p38 phosphorylation in all cell types and to ERK1/2 phosphorylation in 3 of 6 cell types. Furth…

Tumor PhysiologyIntracellular Spacelcsh:MedicineSignal transductionERK signaling cascadeMolecular cell biologyNeoplasmsBasic Cancer ResearchTumor MicroenvironmentSignaling in Cellular ProcessesPhosphorylationCyclic AMP Response Element-Binding ProteinCreb Signalinglcsh:ScienceCellular Stress ResponsesMultidisciplinaryKinaseMechanisms of Signal TransductionSignaling cascadesHydrogen-Ion ConcentrationProtein-Tyrosine KinasesCell biologyOncologyMedicinePhosphorylationMitogen-Activated Protein KinasesSodium-Potassium-Exchanging ATPaseIntracellularResearch ArticleCell SurvivalMAP Kinase Signaling Systemp38 mitogen-activated protein kinasesIntracellular pHBiologyCREBModels BiologicalCell GrowthDogsCell Line TumorAnimalsHumansProtein Kinase InhibitorsBiologyPI3K/AKT/mTOR pathwaylcsh:RRatsEnzyme ActivationCancer cellbiology.proteinlcsh:QExtracellular SpaceReactive Oxygen SpeciesAcidsPLoS ONE
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3'-Untranslated regions of oxidative phosphorylation mRNAs function in vivo, as enhancers of translation

2000

Recent findings have indicated that the 3´-untranslated region (3´-UTR) of the mRNA encoding the β-catalytic subunit of the mitochondrial H+-ATP synthase has an in vitro translation-enhancing activity (TEA) [Izquierdo and Cuezva, Mol. Cell. Biol. (1997) 17, 5255–5268; Izquierdo and Cuezva, Biochem. J. (2000) 346, 849–855]. In the present work, we have expressed chimaeric plasmids that encode mRNA variants of green fluorescent protein in normal rat kidney and liver clone 9 cells to determine whether the 3´-UTRs of nuclear-encoded mRNAs involved in the biogenesis of mitochondria have an intrinsic TEA. TEA is found in the 3´-UTR of the mRNAs encoding the α- and β-subunits of the rat H+-ATP syn…

Untranslated regionTranscription GeneticProtein subunitBlotting WesternGreen Fluorescent ProteinsMitochondrionKidneyTransfectionBiochemistryOxidative PhosphorylationCell LineElectron Transport Complex IVMitochondrial ProteinsMitochondrial transcription factor AGenes ReporterAnimalsCytochrome c oxidaseGreen fluorescent proteinRNA MessengerEnhancer3' Untranslated RegionsMolecular BiologyCell NucleusAU-rich elementMessenger RNAbiologyThree prime untranslated regionNuclear ProteinsCell BiologyH+-ATP synthaseMolecular biologyRatsMitochondriaDNA-Binding ProteinsLuminescent ProteinsProton-Translocating ATPasesLiverMicroscopy FluorescenceProtein Biosynthesisbiology.proteinElectrophoresis Polyacrylamide GelResearch ArticlePlasmidsTranscription FactorsCytochrome c oxidase
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Inhibition by cellular vacuolar ATPase impairs human papillomavirus uncoating and infection.

2014

ABSTRACT Several viruses, including human papillomaviruses, depend on endosomal acidification for successful infection. Hence, the multisubunit enzyme vacuolar ATPase (V-ATPase), which is mainly responsible for endosome acidification in the cell, represents an attractive target for antiviral strategies. In the present study, we show that V-ATPase is required for human papillomavirus (HPV) infection and that uncoating/disassembly but not endocytosis is affected by V-ATPase inhibition. The infection inhibitory potencies of saliphenylhalamide, a proven V-ATPase inhibitor, and its derivatives, as well as those of other V-ATPase inhibitors, were analyzed on different HPV types in relevant cell l…

Vacuolar Proton-Translocating ATPasesEndosomeCell SurvivalCellBiologyAlphapapillomavirusEndocytosisInhibitory postsynaptic potentialAntiviral AgentsCell LineViral ProteinsmedicineHumansPharmacology (medical)Vacuolar ATPasePharmacologychemistry.chemical_classificationVacuolar Proton-Translocating ATPasesVirologyEndocytosisCell biologyInfectious Diseasesmedicine.anatomical_structureEnzymechemistryCell cultureHeLa CellsAntimicrobial agents and chemotherapy
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Targeting V-ATPase in primary human monocytes by archazolid potently represses the classical secretion of cytokines due to accumulation at the endopl…

2014

The macrolide archazolid inhibits vacuolar-type H(+)-ATPase (V-ATPase), a proton-translocating enzyme involved in protein transport and pH regulation of cell organelles, and potently suppresses cancer cell growth at low nanomolar concentrations. In view of the growing link between inflammation and cancer, we investigated whether inhibition of V-ATPase by archazolid may affect primary human monocytes that can promote cancer by sustaining inflammation through the release of tumor-promoting cytokines. Human primary monocytes express V-ATPase, and archazolid (10-100nM) increases the vesicular pH in these cells. Archazolid (10nM) markedly reduced the release of pro-inflammatory (TNF-α, interleuk…

Vacuolar Proton-Translocating ATPasesmedicine.medical_specialtyp38 mitogen-activated protein kinasesInflammationBiologyEndoplasmic ReticulumBiochemistryMonocytesCell Linechemistry.chemical_compoundInternal medicinemedicineHumansSecretionPhosphorylationProtein kinase BDNA PrimersPharmacologyBase SequenceDose-Response Relationship DrugReverse Transcriptase Polymerase Chain ReactionEndoplasmic reticulumBafilomycinCell biologyIκBαEndocrinologySecretory proteinMicroscopy FluorescencechemistryCytokinesMacrolidesmedicine.symptomSignal TransductionBiochemical Pharmacology
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Purified Membrane-Containing Procapsids of Bacteriophage PRD1 Package the Viral Genome

2009

Icosahedral-tailed double-stranded DNA (dsDNA) bacteriophages and herpesviruses translocate viral DNA into a preformed procapsid in an ATP-driven reaction by a packaging complex that operates at a portal vertex. A similar packaging system operates in the tailless dsDNA phage PRD1 (Tectiviridae family), except that there is an internal membrane vesicle in the procapsid. The unit-length linear dsDNA genome with covalently linked 5'-terminal proteins enters the procapsid through a unique vertex. Two small integral membrane proteins, P20 and P22, provide a conduit for DNA translocation. The packaging machinery also contains the packaging ATPase P9 and the packaging efficiency factor P6. Here we…

Viral Plaque AssayvirusesATPaseViral Plaque AssayGenomeViral Proteins03 medical and health scienceschemistry.chemical_compoundCapsidBacteriophage PRD1Structural BiologyBacteriophage PRD1Molecular BiologyIntegral membrane protein030304 developmental biology0303 health sciencesMicrobial Viabilitybiology030306 microbiologyVirus AssemblyCell MembraneMembrane ProteinsMolecular biologyMembranechemistryDNA Viralbiology.proteinBiophysicsTectiviridaeDNAJournal of Molecular Biology
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Creatine kinase is the main target of reactive oxygen species in cardiac myofibrils.

1996

Abstract Reactive oxygen species (ROS) have been reported to alter cardiac myofibrillar function as well as myofibrillar enzymes such as myosin ATPase and creatine kinase (CK). To understand their precise mode and site of action in myofibrils, the effects of the xanthine/xanthine oxidase (X/XO) system or of hydrogen peroxide (H 2 O 2 ) have been studied in the presence and in the absence of phosphocreatine (PCr) in Triton X-100–treated cardiac fibers. We found that xanthine oxidase (XO), with or without xanthine, induced a decrease in maximal Ca 2+ -activated tension. We attributed this effect to the high contaminating proteolytic activity in commercial XO preparations, since it could be p…

Xanthine OxidasebiologyFree RadicalsPhysiologyMyosin ATPaseSuperoxideHydrogen PeroxideMyosinsXanthineMyocardial ContractionPhosphocreatineRatschemistry.chemical_compoundchemistryBiochemistryMyofibrilsbiology.proteinAnimalsCreatine kinasePMSFCardiology and Cardiovascular MedicineMyofibrilXanthine oxidaseReactive Oxygen SpeciesCreatine KinaseCirculation research
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Kinetic modelling of the Zymomonas mobilis Entner-Doudoroff pathway: insights into control and functionality.

2013

Zymomonas mobilis, an ethanol-producing bacterium, possesses the Entner-Doudoroff (E-D) pathway, pyruvate decarboxylase and two alcohol dehydrogenase isoenzymes for the fermentative production of ethanol and carbon dioxide from glucose. Using available kinetic parameters, we have developed a kinetic model that incorporates the enzymic reactions of the E-D pathway, both alcohol dehydrogenases, transport reactions and reactions related to ATP metabolism. After optimizing the reaction parameters within likely physiological limits, the resulting kinetic model was capable of simulating glycolysis in vivo and in cell-free extracts with good agreement with the fluxes and steady-state intermediate …

ZymomonasbiologyEthanolATPaseAlcohol DehydrogenaseGene Expression Regulation BacterialCarbon Dioxidebiology.organism_classificationMicrobiologyZymomonas mobilisModels BiologicalMetabolic engineeringAdenosine TriphosphateGlucoseBiochemistrybiology.proteinGlycolysisComputer SimulationEthanol metabolismEntner–Doudoroff pathwayPyruvate DecarboxylasePyruvate decarboxylaseMetabolic Networks and PathwaysAlcohol dehydrogenaseMicrobiology (Reading, England)
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ISOLATION OF CYTOCHROME OXIDASE COMPLEX FROM SEA URCHIN MITOCHONDRIAL INNER MEMBRANES

1996

Cytochrome oxidase complex has been isolated and purified from sea urchin mitochondrial inner membranes. The complex exhibited a discrete number of bands in PAGE and a 17 kDa band was recognized by an anti-human subunit IV antibody. No bands were recognized by an anti-yeast hsp60 antibody and an anti-sea urchin β ATPase subunit.

animal structuresProtein subunitATPaseCell BiologyGeneral MedicineMitochondrionBiologyMolecular biologyMembraneBiochemistrybiology.animalembryonic structuresbiology.proteinCytochrome c oxidaseHSP60AntibodySea urchinCell Biology International
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