Search results for "RICH"

showing 10 items of 3360 documents

p42 MAPK phosphorylates 80 kDa MARCKS at Ser-113.

1996

Abstract It is demonstrated here that p42 MAPKinase (p42 MAPK) phosphorylates the M yristoylated A lanine- R ich C - K inase S ubstrate (MARCKS) at Ser-113. In permeabilised Swiss 3T3 cells activation of protein kinase C (PKC) leads to p42 MAPK activation, but only the protein kinase C sites in MARCKS become phosphorylated and not Ser-113. The mitogen platelet-derived growth factor (PDGF) elicits the same response. These results demonstrate that while Ser-113 is a substrate for p42 MAPK in vitro and can be phosphorylated in vivo as shown by Taniguchi et al. [(1994) J. Biol. Chem. 269, 18299–18302], its phosphorylation is not subject to acute regulation by p42 MAPK in Swiss 3T3 cells.

MAPK/ERK pathwayMARCKSmedicine.medical_treatmentMitogen-activated protein kinase kinaseBiochemistryenvironment and public healthSubstrate SpecificityMiceStructural BiologySerinep42MAPKinasePhosphorylationMyristoylated Alanine-Rich C Kinase SubstrateCells CulturedProtein Kinase CMitogen-Activated Protein Kinase 1Platelet-Derived Growth FactorbiologyChemistryIntracellular Signaling Peptides and Proteins3T3 CellsProtein-Tyrosine KinasesCell biologyBiochemistryMitogen-activated protein kinasePhosphorylationTetradecanoylphorbol Acetatebiological phenomena cell phenomena and immunityPlatelet-derived growth factor receptorhormones hormone substitutes and hormone antagonistsendocrine systemRecombinant Fusion ProteinsMolecular Sequence DataBiophysicsGeneticsmedicineAnimalsAmino Acid SequenceMARCKSMolecular BiologyProtein kinase CGrowth factorMembrane ProteinsProteinsCell BiologyPeptide FragmentsEnzyme ActivationMolecular Weightenzymes and coenzymes (carbohydrates)Calcium-Calmodulin-Dependent Protein Kinasesbiology.proteinMutagenesis Site-DirectedMitogensFEBS letters
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Global Functional Analyses of Cellular Responses to Pore-Forming Toxins

2011

Here we present the first global functional analysis of cellular responses to pore-forming toxins (PFTs). PFTs are uniquely important bacterial virulence factors, comprising the single largest class of bacterial protein toxins and being important for the pathogenesis in humans of many Gram positive and Gram negative bacteria. Their mode of action is deceptively simple, poking holes in the plasma membrane of cells. The scattered studies to date of PFT-host cell interactions indicate a handful of genes are involved in cellular defenses to PFTs. How many genes are involved in cellular defenses against PFTs and how cellular defenses are coordinated are unknown. To address these questions, we pe…

MAPK/ERK pathwayTranscription GeneticImmunology/Innate ImmunityMessengerInteractomeInfectious Diseases/Bacterial InfectionsRNA interference2.1 Biological and endogenous factorsAetiologyBiology (General)Genes HelminthCaenorhabditis elegansOligonucleotide Array Sequence AnalysisGenetics0303 health sciencesGenomebiologyReverse Transcriptase Polymerase Chain ReactionGenetics and Genomics/Functional Genomics030302 biochemistry & molecular biologyrespiratory systemCell biologyInfectious DiseasesMedical MicrobiologyRNA InterferenceSignal transductionDNA microarrayTranscriptionBiotechnologyResearch ArticleSignal TransductionPore Forming Cytotoxic ProteinsQH301-705.5Virulence FactorsMAP Kinase Signaling System1.1 Normal biological development and functioningBacterial ToxinsImmunologyMicrobiologyDNA-binding proteinCell Line03 medical and health sciencesBacterial ProteinsGeneticUnderpinning researchVirologyEscherichia coliHelminthGeneticsAnimalsHumansRNA MessengerCaenorhabditis elegansCaenorhabditis elegans ProteinsMolecular BiologyGene030304 developmental biologyGenome HelminthCell MembraneGenetics and GenomicsRC581-607biology.organism_classificationrespiratory tract diseasesTranscription Factor AP-1Emerging Infectious DiseasesGenesRNAParasitologyGeneric health relevanceRNA HelminthImmunologic diseases. AllergyPLoS Pathogens
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Effect of reducing agents on the acidification capacity and the proton motive force of Lactococcus lactis ssp. cremoris resting cells.

2002

International audience; Reducing agents are potential inhibitors of the microbial growth. We have shown recently that dithiothreitol (DTT), NaBH(4) and H(2) can modify the proton motive force of resting cells of Escherichia coli by increasing the membrane protons permeability [Eur. J. Biochem. 262 (1999) 595]. In the present work, the effect of reducing agents on the resting cells of Lactococcus lactis ssp. cremoris, a species widely employed in dairy processes was investigated. DTT did not affect the acidification nor the DeltapH, in contrast to the effect previously reported on E. coli. The DeltaPsi was slightly increased (30 mV) at low pH (pH 4) in the presence of 31 mM DTT or 2.6 mM NaB…

MESH : Cell LineMESH: Hydrogen-Ion ConcentrationMESH : DithioniteBorohydridesMESH : DithiothreitolBacterial growthmedicine.disease_causeMESH: Proton-Motive ForceDithiothreitolSodium dithionitechemistry.chemical_compoundMESH : Proton-Motive ForceElectrochemistry[INFO.INFO-BT]Computer Science [cs]/Biotechnology0303 health sciencesMESH : Interphasebiologyfood and beveragesProton-Motive ForceGeneral MedicineHydrogen-Ion ConcentrationMESH: BorohydridesLactococcus lactisMembraneBiochemistryReducing AgentsMESH : Sensitivity and SpecificityMESH : Reducing Agents[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyReducing agentMESH: Reducing AgentsBiophysics[SDV.BC]Life Sciences [q-bio]/Cellular BiologySensitivity and SpecificityCell LineMESH: Interphase03 medical and health sciencesSpecies SpecificityMESH : Hydrogen-Ion ConcentrationMESH: DithionitemedicineMESH : Species SpecificityMESH: Species SpecificityLactic AcidPhysical and Theoretical ChemistryEscherichia coli[SDV.BC] Life Sciences [q-bio]/Cellular BiologyInterphase030304 developmental biology[ SDV.BC ] Life Sciences [q-bio]/Cellular Biology030306 microbiologyChemiosmosisLactococcus lactisDithionitebiology.organism_classificationMESH: Sensitivity and SpecificityMESH: Cell LineDithiothreitol[INFO.INFO-BT] Computer Science [cs]/BiotechnologychemistryMESH: Lactococcus lactisMESH : BorohydridesMESH : Lactic AcidBiophysicsMESH: Lactic AcidMESH : Lactococcus lactisMESH: Dithiothreitol
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Evaluation of acyl coenzyme A oxidase (Aox) isozyme function in the n- alkane-assimilating yeast Yarrowia lipolytica

1999

ABSTRACT We have identified five acyl coenzyme A (CoA) oxidase isozymes (Aox1 through Aox5) in the n -alkane-assimilating yeast Yarrowia lipolytica , encoded by the POX1 through POX5 genes. The physiological function of these oxidases has been investigated by gene disruption. Single, double, triple, and quadruple disruptants were constructed. Global Aox activity was determined as a function of time after induction and of substrate chain length. Single null mutations did not affect growth but affected the chain length preference of acyl-CoA oxidase activity, as evidenced by a chain length specificity for Aox2 and Aox3. Aox2 was shown to be a long-chain acyl-CoA oxidase and Aox3 was found to …

MESH : Escherichia coliMESH: Sequence Analysis DNAMESH : Molecular Sequence DataMutantGene ExpressionMESH: Base Sequencechemistry.chemical_compoundCloning Molecular[INFO.INFO-BT]Computer Science [cs]/BiotechnologyDNA FungalMESH: MutagenesisMESH : IsoenzymesOxidase testbiologyMESH: Escherichia coliMESH: Acyl-CoA OxidaseMESH : MutagenesisMESH : Cell DivisionMESH : OxidoreductasesIsoenzymesBlotEukaryotic Cells[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyFungalBiochemistryMESH: IsoenzymesMESH: Cell DivisionMESH : Acyl-CoA OxidaseOxidoreductasesSequence Analysis[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyCell DivisionMESH: Gene ExpressionMESH : Cloning MolecularGenes FungalMolecular Sequence DataMicrobiologyIsozymeWESTERN BLOTTINGAlkanes[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyEscherichia coliMESH: Cloning Molecular[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH: OxidoreductasesMESH: Saccharomycetales[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMolecular BiologyGeneMESH : AlkanesMESH: Molecular Sequence DataBase SequenceMolecularYarrowiaSequence Analysis DNAMESH : SaccharomycetalesDNAbiology.organism_classificationMolecular biologyYeastMESH : Gene ExpressionMESH: AlkanesMESH: DNA FungalOleic acid[INFO.INFO-BT] Computer Science [cs]/BiotechnologyGeneschemistryMutagenesisSaccharomycetalesMESH : Base SequenceMESH : Genes FungalAcyl-CoA OxidaseMESH : DNA FungalMESH: Genes FungalMESH : Sequence Analysis DNACloning
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Extracellular oxidoreduction potential modifies carbon and electron flow in Escherichia coli.

2000

ABSTRACT Wild-type Escherichia coli K-12 ferments glucose to a mixture of ethanol and acetic, lactic, formic, and succinic acids. In anoxic chemostat culture at four dilution rates and two different oxidoreduction potentials (ORP), this strain generated a spectrum of products which depended on ORP. Whatever the dilution rate tested, in low reducing conditions (−100 mV), the production of formate, acetate, ethanol, and lactate was in molar proportions of approximately 2.5:1:1:0.3, and in high reducing conditions (−320 mV), the production was in molar proportions of 2:0.6:1:2. The modification of metabolic fluxes was due to an ORP effect on the synthesis or stability of some fermentation enzy…

MESH : Models Chemical0106 biological sciencesMESH: Oxidation-ReductionMESH : Acetic AcidMESH : Escherichia coliMESH : NADFormatesOxaloacetatesMESH: Phosphoenolpyruvate CarboxylaseSuccinic AcidMESH: Alcohol DehydrogenaseMESH : CarbonMESH : EthanolMESH: Carbon Dioxide01 natural sciencesPhosphoenolpyruvatechemistry.chemical_compoundModels[INFO.INFO-BT]Computer Science [cs]/BiotechnologyAcetic Acid0303 health sciencesbiologyMESH: Escherichia coliMESH: Models ChemicalMESH : Acetyl Coenzyme AMESH: NADLactic acidMESH : Carbon DioxideBiochemistryFormic AcidsMESH: PhosphoenolpyruvateMESH: Acetic AcidMESH: Pyruvate KinaseMESH : Phosphoenolpyruvate CarboxylaseMESH: Oxaloacetic AcidsOxidation-Reduction[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyMESH: EthanolPhysiology and MetabolismPyruvate KinaseElectronsChemicalMESH: CarbonMESH : Formic AcidsChemostatMicrobiologyMESH: Fermentation03 medical and health sciencesAcetic acidMESH : Alcohol DehydrogenaseAcetyl Coenzyme AMESH : Fermentation010608 biotechnology[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyEscherichia coliFormate[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyLactic Acid[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMolecular Biology030304 developmental biologyAlcohol dehydrogenaseMESH : Oxidation-ReductionMESH: ElectronsEthanolEthanolMESH : Succinic AcidAlcohol DehydrogenaseCarbon DioxideNADMESH: Formic AcidsMESH : Pyruvate KinaseCarbonOxaloacetic AcidsPhosphoenolpyruvate CarboxylaseMESH: Succinic Acid[INFO.INFO-BT] Computer Science [cs]/BiotechnologychemistryModels ChemicalSuccinic acidMESH : Lactic AcidMESH : Oxaloacetic AcidsFermentationbiology.proteinFermentationMESH: Lactic AcidMESH : ElectronsMESH : PhosphoenolpyruvateMESH: Acetyl Coenzyme A
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Virulent synergistic effect between Enterococcus faecalis and Escherichia coli assayed by using the Caenorhabditis elegans model.

2008

5 pages; International audience; BACKGROUND: The role of enterococci in the pathogenesis of polymicrobial infections is still debated. The purpose of this study was to evaluate the effect of virulent enterococci in the presence or absence of Escherichia coli strains in the in vivo Caenorhabditis elegans model. PRINCIPAL FINDINGS: This study demonstrated that there was a synergistic effect on virulence when an association of enterococci and E. coli (LT50 = 1.6 days+/-0.1 according to the tested strains and death of nematodes in 4 days+/-0.5) was tested in comparison with enterococci alone (LT50 = 4.6 days+/-0.1 and death in 10.4 days+/-0.6) or E. coli alone (LT50 = 2.1+/-0.9 and deaths 6.6+/…

MESH : Virulence FactorsInfectious Diseases/Gastrointestinal InfectionsMESH : Escherichia colilcsh:MedicineMESH : Genotypemedicine.disease_causeMESH: Regression AnalysisPathogenesisMESH: GenotypeInfectious Diseases/Bacterial InfectionsMESH : Regression AnalysisGenotype[ SDV.EE.IEO ] Life Sciences [q-bio]/Ecology environment/SymbiosisEnterococcus faecalis[ SDV.IMM ] Life Sciences [q-bio]/ImmunologyMESH: AnimalsMESH : Anti-Bacterial AgentsMESH : Enterococcus faecalislcsh:ScienceCaenorhabditis elegans0303 health sciencesMultidisciplinarybiologyMESH: Escherichia coliBacterial Infections3. Good healthAnti-Bacterial AgentsMicrobiology/Immunity to InfectionsMESH : Bacterial InfectionsGastroenterology and Hepatology/Gastrointestinal Infections[SDV.IMM]Life Sciences [q-bio]/ImmunologyRegression AnalysisMicrobiology/Cellular Microbiology and PathogenesisResearch ArticleMESH: Enterococcus faecalis[SDV.IMM] Life Sciences [q-bio]/ImmunologyGenotypeMESH: Bacterial InfectionsVirulence FactorsVirulenceEnterococcus faecalisMicrobiologyMESH : Caenorhabditis elegans03 medical and health sciencesIn vivoMESH: Anti-Bacterial AgentsMESH: Caenorhabditis elegansmedicineEscherichia coliAnimalsCaenorhabditis elegansEscherichia coli030304 developmental biologyMESH: Virulence Factors030306 microbiologylcsh:RMicrobiology/Medical Microbiology[SDV.EE.IEO] Life Sciences [q-bio]/Ecology environment/Symbiosisbiology.organism_classificationMESH : Disease Models AnimalDisease Models AnimalEnterococcuslcsh:QMESH : AnimalsMESH: Disease Models Animal[SDV.EE.IEO]Life Sciences [q-bio]/Ecology environment/SymbiosisPloS one
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Genetics for Pseudoalteromonas provides tools to manipulate marine bacterial virus PM2

2008

ABSTRACT The genetic manipulation of marine double-stranded DNA (dsDNA) bacteriophage PM2 ( Corticoviridae ) has been limited so far. The isolation of an autonomously replicating DNA element of Pseudoalteromonas haloplanktis TAC125 and construction of a shuttle vector replicating in both Escherichia coli and Pseudoalteromonas enabled us to design a set of conjugative shuttle plasmids encoding tRNA suppressors for amber mutations. Using a host strain carrying a suppressor plasmid allows the introduction and analysis of nonsense mutations in PM2. Here, we describe the isolation and characterization of a suppressor-sensitive PM2 sus2 mutant deficient in the structural protein P10. To infect an…

MESH: Corticoviridae[SDV]Life Sciences [q-bio]Bacteriophages Transposons and PlasmidsMutantPlasmidPseudoalteromonasRNA TransferMESH: Genetic VectorsMESH: Models GeneticMESH: Capsid ProteinsGenetics0303 health sciencesbiologyMESH: Escherichia coliPseudoalteromonasMESH: Mutagenesis Site-DirectedPhenotypeMESH: DNA CircularElectrophoresis Polyacrylamide GelDNA CircularMESH: Genome ViralPlasmidsMESH: MutationGenetic VectorsGenome ViralMESH: PhenotypeMicrobiologyPseudoalteromonas haloplanktisViral Proteins03 medical and health sciencesShuttle vectorMESH: PlasmidsHost outer membraneEscherichia coliSeawaterMolecular Biology030304 developmental biologyModels Genetic030306 microbiologyMESH: PseudoalteromonasCorticoviridaeMESH: SeawaterViral membranebiology.organism_classificationMESH: RNA TransferMESH: Viral Proteins[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyMutationMutagenesis Site-DirectedCapsid ProteinsBacterial virusMESH: Electrophoresis Polyacrylamide Gel
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Combined action of redox potential and pH on heat resistance and growth recovery of sublethally heat-damaged Escherichia coli

2000

International audience; The combined effect of redox potential (RP) (from -200 to 500 mV) and pH (from 5.0 to 7.0) on the heat resistance and growth recovery after heat treatment of Escherichia coli was tested. The effect of RP on heat resistance was very different depending on the pH. At pH 6.0, there was no significant difference, whereas at pH 5.0 and 7.0 maximum resistance was found in oxidizing conditions while it fell in reducing ones. In sub-lethally heat-damaged cells, low reducing and acid conditions allowed growth ability to be rapidly regained, but a decrease in the redox potential and pH brought about a longer lag phase and a slower exponential growth rate, and even led to growt…

MESH: Oxidation-ReductionMESH : Escherichia coliMESH: Hydrogen-Ion ConcentrationHot TemperatureThermal resistanceMESH: Hot Temperaturemedicine.disease_causeApplied Microbiology and BiotechnologyRedox03 medical and health sciencesExponential growthMESH : Hydrogen-Ion Concentration[ SDV.MP ] Life Sciences [q-bio]/Microbiology and ParasitologyOxidizing agentEscherichia colimedicineGrowth rate[INFO.INFO-BT]Computer Science [cs]/Biotechnology[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyEscherichia coliComputingMilieux_MISCELLANEOUS030304 developmental biologyMESH : Oxidation-Reduction0303 health sciencesbiologyMESH: Escherichia coli030306 microbiologyChemistryGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationEnterobacteriaceaeCulture Media[INFO.INFO-BT] Computer Science [cs]/Biotechnology[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyBiochemistryMESH: Culture MediaBiophysicsMESH : Culture MediaMESH : Hot TemperatureOxidation-Reduction[ INFO.INFO-BT ] Computer Science [cs]/BiotechnologyBacteriaBiotechnologyApplied Microbiology and Biotechnology
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Changes in the proton-motive force in Escherichia coli in response to external oxidoreduction potential.

1999

International audience; The pH homeostasis and proton-motive force (Deltap) of Escherichia coli are dependent on the surrounding oxidoreduction potential (ORP). Only the internal pH value and, thus, the membrane pH gradient (DeltapH) component of the Deltap is modified, while the membrane potential (DeltaPsi) does not change in a significant way. Under reducing conditions (Eh < 50 mV at pH 7.0), E. coli decreases its Deltap especially in acidic media (21% decrease at pH 7.0 and 48% at pH 5.0 for a 850-mV ORP decrease). Measurements of ATPase activity and membrane proton conductance (CH+m) depending on ORP and pH have shown that the internal pH decrease is due to an increase in membrane prot…

MESH: Oxidation-ReductionMESH : Escherichia coliMESH: Hydrogen-Ion ConcentrationMembrane permeabilitymedicine.disease_causeBiochemistryMembrane Potentials03 medical and health sciencesMESH : Hydrogen-Ion Concentration[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologymedicineEscherichia coliMESH: Adenosine TriphosphatasesMESH : Membrane PotentialsMESH : ProtonsMESH: Membrane Potentials[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular Biology[INFO.INFO-BT]Computer Science [cs]/Biotechnology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyEscherichia coliComputingMilieux_MISCELLANEOUS030304 developmental biologyMESH : Oxidation-ReductionMembrane potentialchemistry.chemical_classificationAdenosine Triphosphatases0303 health sciencesChromatographyMESH : Adenosine Triphosphatases030306 microbiologyChemiosmosisChemistryMESH: Escherichia coliConductanceHydrogen-Ion Concentration[INFO.INFO-BT] Computer Science [cs]/BiotechnologyMembranePermeability (electromagnetism)BiophysicsThiolMESH: ProtonsProtonsOxidation-Reduction[ INFO.INFO-BT ] Computer Science [cs]/Biotechnology
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Sicurezza dell’Infliximab in bambini con malattia infiammatoria cronica intestinale (IBD): Registro pediatrico italiano di terapia biologica per le I…

2008

MICI PediatricheInfliximab
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