Search results for "(Escherichia coli)"

showing 10 items of 689 documents

O2 as the regulatory signal for FNR-dependent gene regulation in Escherichia coli

1996

With an oxystat, changes in the pattern of expression of FNR-dependent genes from Escherichia coli were studied as a function of the O2 tension (pO2) in the medium. Expression of all four tested genes was decreased by increasing O2. However, the pO2 values that gave rise to half-maximal repression (pO(0.5)) were dependent on the particular promoter and varied between 1 and 5 millibars (1 bar = 10(5) Pa). The pO(0.5) value for the ArcA-regulated succinate dehydrogenase genes was in the same range (pO(0.5) = 4.6 millibars). At these pO2 values, the cytoplasm can be calculated to be well supplied with O2 by diffusion. Therefore, intracellular O2 could provide the signal to FNR, suggesting that…

Iron-Sulfur ProteinsCellular respirationRepressorBiologymedicine.disease_causeMicrobiologyElectron TransportBacterial ProteinsGenes RegulatorEscherichia colimedicineAnaerobiosisMolecular BiologyEscherichia coliRegulation of gene expressionchemistry.chemical_classificationEscherichia coli ProteinsSuccinate dehydrogenaseMembrane ProteinsGene Expression Regulation BacterialElectron transport chainAerobiosisOxygenRepressor ProteinsSuccinate DehydrogenaseEnzymeLac OperonchemistryBiochemistryGenes BacterialMutationbiology.proteinOxidation-ReductionProtein KinasesIntracellularBacterial Outer Membrane ProteinsSignal TransductionResearch ArticleJournal of Bacteriology
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The Friedreich's Ataxia protein frataxin modulates DNA base excision repair in prokaryotes and mammals

2010

DNA-repair mechanisms enable cells to maintain their genetic information by protecting it from mutations that may cause malignant growth. Recent evidence suggests that specific DNA-repair enzymes contain ISCs (iron–sulfur clusters). The nuclearencoded protein frataxin is essential for the mitochondrial biosynthesis of ISCs. Frataxin deficiency causes a neurodegenerative disorder named Friedreich's ataxia in humans. Various types of cancer occurring at young age are associated with this disease, and hence with frataxin deficiency. Mice carrying a hepatocyte-specific disruption of the frataxin gene develop multiple liver tumours for unresolved reasons. In the present study, we show that frata…

Iron-Sulfur ProteinsDNA Repairmedicine.disease_causeBiochemistryDNA Glycosylases8-oxoG 78-dihydro-8-oxoguanineMice0302 clinical medicineIron-Binding Proteinsoxidative stressBER base excision repairCells CulturedMammalsMice Knockout0303 health sciencesfrataxinDMEM Dulbecco's modified Eagle's mediumbiologyLiver NeoplasmsSalmonella entericairon–sulfur clusterLife SciencesIron-binding proteinsTransfection3. Good healthLB Luria–BertaniOGG1 8-oxoguanine DNA glycosylase 1ISC iron–sulfur clusterFpg formamido-pyrimidine DNA glycosylaseHPRT hypoxanthine phosphoribosyltransferaseResearch ArticleDNA damageDNA repairSSB DNA single-strand breakTransfectionCell Line03 medical and health sciencesFRDA Friedreich's ataxiaROS reactive oxygen speciesmedicineAnimalsHumansMUTYH human mutY homologue (Escherichia coli)Molecular BiologyGene030304 developmental biologyFriedreich's ataxiaCell BiologyFibroblastsMolecular biologytumorigenesisProkaryotic CellsFriedreich AtaxiaDNA base excision repairDNA glycosylaseMutationHepatocytesFrataxinbiology.proteinInstitut für ErnährungswissenschaftCarcinogenesisMAPK mitogen-activated protein kinase030217 neurology & neurosurgeryDNA Damage
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O2-sensing and O2-dependent gene regulation in facultatively anaerobic bacteria.

1995

Availability of O2 is one of the most important regulatory signals in facultatively anaerobic bacteria. Various two- or one-component sensor/regulator systems control the expression of aerobic and anaerobic metabolism in response to O2. Most of the sensor proteins contain heme or Fe as cofactors that interact with O2 either by binding or by a redox reaction. The ArcA/ArcB regulator of aerobic metabolism in Escherichia coli may use a different sensory mechanism. In two-component regulators, the sensor is located in the cytoplasmic membrane, whereas one-component regulators are located in the cytoplasm. Under most conditions, O2 can readily reach the cytoplasm and could provide the signal in …

Iron-Sulfur ProteinsGram-Negative Facultatively Anaerobic RodsAnaerobic respirationRegulatorBiologymedicine.disease_causeBiochemistryMicrobiologychemistry.chemical_compoundBacterial ProteinsGeneticsmedicineMolecular BiologyHemeEscherichia coliRegulation of gene expressionSensory mechanismEscherichia coli ProteinsGeneral MedicineGene Expression Regulation Bacterialbiology.organism_classificationOxygenchemistryBiochemistrybacteriaAnaerobic bacteriaBacteriaTranscription FactorsArchives of microbiology
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Stimulation of Fe-S cluster insertion into apoFNR by Escherichia coli glutaredoxins 1, 2 and 3 in vitro.

2004

Abstract The oxygen sensor fumarate nitrate reductase regu-lator (FNR) of Escherichia coli contains in the active (anaerobic)state a [4Fe–4S] 2þ cluster which is lost after exposure to O 2 .Inaerobically prepared apoFNR, or in FNR obtained by treatmentof [4Fe–4S] FNR with O 2 in vitro, intramolecular cysteinedisulfides are found, including the cysteine residues which serveas ligands for the Fe–S cluster. It is shown here that thereconstitution of [4Fe–4S] FNR from this form of aerobicapoFNR was preceded by a long lag phase when glutathione wasused as the reducing agent. Addition of E. coli glutaredoxins(Grx) 1, 2 or 3 decreased the lag phase greatly and stimulatedthe reconstitution rate slig…

Iron-Sulfur ProteinsTime FactorsReducing agentFNRGlutaredoxinBiophysicsBiologyReductaseSulfidesmedicine.disease_causeNitrate reductaseBiochemistryOxygen sensorchemistry.chemical_compoundStructural BiologyGlutaredoxinGeneticsmedicineEscherichia coliCysteineDisulfidesThioredoxinMolecular BiologyEscherichia coliGlutaredoxinsDisulfide reductaseEscherichia coli ProteinsProteinsCell BiologyGlutathioneGlutathioneOxygenBiochemistrychemistryMultigene FamilyThioredoxinOxidoreductasesCysteineTranscription FactorsFEBS letters
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The oxygen-responsive transcriptional regulator FNR ofEscherichia coli : the search for signals and reactions

1997

The FNR (fumarate and nitrate reductase regulation) protein of Escherichia coli is an oxygen-responsive transcriptional regulator required for the switch from aerobic to anaerobic metabolism. In the absence of oxygen, FNR changes from the inactive to the active state. The sensory and the regulatory functions reside in separate domains of FNR. The sensory domain contains a Fe-S cluster, which is of the [4Fe-4S]2+ type under anaerobic conditions. It is suggested that oxygen is supplied to the cytoplasmic FNR by diffusion and inactivates FNR by direct interaction. Reactivation under anoxic conditions requires cellular reductants. In vitro, the Fe-S cluster is converted to a [3Fe-4S]+ or a [2Fe…

Iron-Sulfur Proteinsinorganic chemicalsEscherichia coli Proteinschemistry.chemical_elementBiologyNitrate reductasemedicine.disease_causeenvironment and public healthMicrobiologyOxygenMetabolic pathwayBacterial ProteinschemistryBiochemistryCytoplasmRespirationEscherichia coliTranscriptional regulationmedicinebacteriaSignal transductionMolecular BiologyEscherichia coliSignal TransductionTranscription FactorsMolecular Microbiology
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Hydrogen-producingEscherichia colistrains overexpressing lactose permease: FT-IR analysis of the lactose-induced stress

2014

The lactose permease gene (lacY) was overexpressed in the septuple knockout mutant of Escherichia coli, previously engineered for hydrogen production from glucose. It was expected that raising the lactose transporter activity would elevate the intracellular lactose concentration, inactivate the lactose repressor, induce the lactose operon, and as a result stimulate overall lactose consumption and conversion. However, overexpression of the lactose transporter caused a considerable growth delay in the recombinant strain on lactose, resembling to some extent the "lactose killing" phenomenon. Therefore, the recombinant strain was subjected to selection on lactose-containing media. Selection on …

Lactose permeasebiologyProcess Chemistry and TechnologyMutantBiomedical Engineeringlac operonBioengineeringGeneral MedicineLac repressormedicine.disease_causeApplied Microbiology and Biotechnologylaw.inventionchemistry.chemical_compoundBiochemistrychemistrylawDrug DiscoverymedicineRecombinant DNAAlpha-lactalbuminbiology.proteinMolecular MedicineLactoseEscherichia coliBiotechnologyBiotechnology and Applied Biochemistry
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Tetracycline inhibits the nitric oxide synthase activity induced by endotoxin in cultured murine macrophages

1998

Here we investigate the effects of tetracycline base and of a semi-synthetic tetracycline derivative, doxycycline, on the induction of inducible nitric oxide synthase and, hence, on the production of nitric oxide (NO) by lipopolysaccharide in J774 macrophage cultured in vitro. The treatment of J774 line with tetracycline base (6.25-250 microM) or doxycycline (5-50 microM) dose-dependently decreased the lipopolysaccharide-stimulated (1 microg/ml) inducible NO synthase activity and, consequently, nitrite formation. For instance, the inhibition was 70% for tetracycline base at 250 microM and 68% for doxycycline at 50 microM. The inhibitory effect of tetracyclines was due neither to a reduction…

LipopolysaccharideCell SurvivalTetracyclineBlotting WesternNitric Oxide Synthase Type IINitric oxideMicechemistry.chemical_compoundWestern blotPolysaccharidesEscherichia colimedicineAnimalsRNA MessengerAntibacterial agentPharmacologyDoxycyclinebiologymedicine.diagnostic_testMacrophagesBiological activityTetracyclineAnti-Bacterial AgentsEndotoxinsNitric oxide synthaseBiochemistrychemistryDoxycyclineEnzyme InductionProtein Biosynthesisbiology.proteinElectrophoresis Polyacrylamide GelNitric Oxide Synthasemedicine.drugEuropean Journal of Pharmacology
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Effects of Escherichia coli hemolysin on human monocytes. Cytocidal action and stimulation of interleukin 1 release.

1990

Abstract This study reports on the potent cytocidal and interleukin-1 releasing properties of Escherichia coli hemolysin (ECH) on human monocytes. Nanomolar concentrations of purified ECH (250-2,000 ng/ml) caused rapid and irreversible depletion of cellular ATP to levels below 20% of controls within 60 min. Subcytocidal doses (10-200 ng/ml) of ECH induced rapid release within 60-120 min of large amounts of interleukin 1 beta (IL-1 beta) from cultured monocytes. IL-1 beta release occurred in the presence of actinomycin D and cycloheximide, and was thus probably due to processing and export of intracellular IL-1 beta precursor. Incubation of toxin-producing E. coli at ratios of only 0.3-3 col…

LipopolysaccharidesCell SurvivalStimulationIn Vitro TechniquesBiologyCycloheximidemedicine.disease_causeHemolysin ProteinsMonocytesMicrobiologyHemolysin Proteinschemistry.chemical_compoundAdenosine TriphosphateEscherichia colimedicineHumansEscherichia coliCells CulturedToxinMonokinesMonocyteInterleukinDrug SynergismGeneral Medicinemedicine.anatomical_structurechemistrySecretory RateIntracellularResearch ArticleInterleukin-1Journal of Clinical Investigation
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The Host Response toListeria monocytogenesMutants Defective in Genes Encoding Phospholipases C(plcA, plcB)and Actin Assembly(actA)

1997

Several genes involved in the determination of Listeria monocytogenes pathogenesis have been identified. Among them, plcA gene encodes phosphatidylinositol-specific phospholipase C (PI-PLC), plcB gene encodes a broad-range phospholipase C (PC-PLC), and actA encodes a protein contributing to actin assembly in infected cells. The interaction of L. monocytogenes wild type (LO 28) strain and two derivative mutants, plcA- (BUG 206) and actA-/plcB- (LUT 12), with macrophages and T lymphocytes was investigated in a mouse model of listeriosis. Both mutants showed evidence of attenuation. The plcA- mutant, but not the plcB- mutant, expressed an increase in susceptibility to the anti-listerial activi…

LipopolysaccharidesCellular immunityT-LymphocytesImmunologyMutantDose-Response Relationship ImmunologicBiologyLymphocyte ActivationPhosphatidylinositolsmedicine.disease_causeMicrobiologyMicrobiologyMicePhagocytosisListeria monocytogenesVirologyEscherichia colimedicineAnimalsListeriosisGeneEscherichia coliCells CulturedMice Inbred BALB CPhospholipase CWild typeInterleukin-12Listeria monocytogenesActinsGenes BacterialType C PhospholipasesMutationMacrophages PeritonealInterleukin 12FemaleSpleenMicrobiology and Immunology
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COMPLEMENT-DEPENDENT B-CELL ACTIVATION BY COBRA VENOM FACTOR AND OTHER MITOGENS?

1974

It has been proposed that two distinct signals are required for the triggering of the precursors of antibody-forming bone marrow-derived cells (B cells): (a) the binding of antigen or of a mitogen to the corresponding receptor sites on B-cell membranes and (b) the interaction of activated C3 with the C3 receptor of B lymphocytes. There is growing evidence that B-cell mitogens and T (thymus-derived cell)-independent antigens are capable of activating the alternate pathway of the complement system (bypass). Therefore, the effect of another potent bypass inducer was investigated with regard to B-cell activation and the role of C3. Purified, pyrogen-free cobra venom factor was mitogenic for bot…

LipopolysaccharidesErythrocytesT-LymphocytesImmunologyHemolytic Plaque TechniqueMice Inbred StrainsLymphocyte ActivationTritiumArticleMiceAntigenPolysaccharidesLectinsConcanavalin AEscherichia coliAnimalsImmunology and AllergyCells CulturedImmune adherence reactionAntigens BacterialB-LymphocytesSheepbiologyVenomsPokeweed mitogenSnakesComplement System ProteinsMolecular biologyImmune Adherence ReactionComplement systemKineticsCell cultureConcanavalin AAntibody Formationbiology.proteinMitogensAntibodyFetal bovine serumThymidineJournal of Experimental Medicine
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