Search results for "Escherichia coli K12"

showing 8 items of 8 documents

Cryopreservation of Escherichia coli K12TG1: Protection from the damaging effects of supercooling by freezing

2015

Injuries in living cells caused by water freezing during a freeze-thaw process have been extensively reported. In particular, intracellular water freezing has long been incriminated in cell death caused by a high cooling rate, but this supposition could not always be demonstrated. This work aims to discriminate the role of water freezing, dehydration and cold-induced injuries in cellular damage occuring during cryopreservation. For this purpose, Escherichia coli K12TG1 suspensions were maintained in a supercooled or frozen state at -20°C for times ranging from 10 min to 5 h. The supercooled state was maintained for a long period at -20°C by applying a non-injurious isostatic pressure (P<40 …

Cell Membrane PermeabilityCell SurvivalGeneral Biochemistry Genetics and Molecular BiologyCryopreservationchemistry.chemical_compoundCryoprotective AgentsFreezingmedicineOsmotic pressureDehydrationPropidium iodideSupercoolingFluorescent DyesCryopreservationChromatographyCell DeathDehydrationEscherichia coli K12ChemistryCell MembraneIceGeneral MedicineThiobarbituratesmedicine.diseaseMembraneBiophysicsGeneral Agricultural and Biological SciencesLaurdanIntracellularPropidiumCryobiology
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Damage in Escherichia coli Cells Treated with a Combination of High Hydrostatic Pressure and Subzero Temperature

2007

ABSTRACT The relationship between membrane permeability, changes in ultrastructure, and inactivation in Escherichia coli strain K-12TG1 cells subjected to high hydrostatic pressure treatment at room and subzero temperatures was studied. Propidium iodide staining performed before and after pressure treatment made it possible to distinguish between reversible and irreversible pressure-mediated cell membrane permeabilization. Changes in cell ultrastructure were studied using transmission electron microscopy (TEM), which showed noticeable condensation of nucleoids and aggregation of cytosolic proteins in cells fixed after decompression. A novel technique used to mix fixation reagents with the c…

Cell Membrane PermeabilityMembrane permeability[SDV]Life Sciences [q-bio]CellHydrostatic pressureColony Count MicrobialApplied Microbiology and BiotechnologyCell membrane03 medical and health scienceschemistry.chemical_compound[SPI]Engineering Sciences [physics]Microscopy Electron TransmissionFreezing[ SPI ] Engineering Sciences [physics]medicineHydrostatic PressureNucleoidPropidium iodideComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciences[ SDV ] Life Sciences [q-bio]EcologyEscherichia coli K12030306 microbiologyTemperaturePhysiology and BiotechnologyCulture MediaCytosolmedicine.anatomical_structurechemistryBiochemistryMicroscopy FluorescenceBiophysicsUltrastructureFood ScienceBiotechnology
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Topology and accessibility of the transmembrane helices and the sensory site in the bifunctional transporter DcuB of Escherichia coli.

2011

C(4)-Dicarboxylate uptake transporter B (DcuB) of Escherichia coli is a bifunctional transporter that catalyzes fumarate/succinate antiport and serves as a cosensor of the sensor kinase DcuS. Sites and domains of DcuB were analyzed for their topology relative to the cytoplasmic or periplasmic side of the membrane and their accessibility to the water space. For the topology studies, DcuB was fused at 33 sites to the reporter enzymes PhoA and LacZ that are only active when located in the periplasm or the cytoplasm, respectively. The ratios of the PhoA and LacZ activities suggested the presence of 10 or 11 hydrophilic loops, and 11 or 12 α-helical transmembrane domains (TMDs). The central part…

Models MolecularRecombinant Fusion ProteinsMolecular Sequence Datalac operonTopologyBiochemistryProtein Structure SecondaryPolyethylene GlycolsProtein structureBacterial ProteinsCatalytic DomainStilbenesAmino Acid SequenceCysteineBinding sitePeptide sequenceDicarboxylic Acid TransportersEscherichia coli K12ChemistryEscherichia coli ProteinsCell MembranePeriplasmic spaceAlkaline PhosphataseTransmembrane domainMembrane proteinBiochemistryLac OperonEthylmaleimideSulfonic AcidsHydrophobic and Hydrophilic InteractionsCysteineBiochemistry
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Regulation of aerobic and anaerobic D-malate metabolism of Escherichia coli by the LysR-type regulator DmlR (YeaT).

2010

ABSTRACT Escherichia coli K-12 is able to grow under aerobic conditions on d -malate using DctA for d -malate uptake and the d -malate dehydrogenase DmlA (formerly YeaU) for converting d -malate to pyruvate. Induction of dmlA encoding DmlA required an intact dmlR (formerly yeaT ) gene, which encodes DmlR, a LysR-type transcriptional regulator. Induction of dmlA by DmlR required the presence of d -malate or l - or meso -tartrate, but only d -malate supported aerobic growth. The regulator of general C 4 -dicarboxylate metabolism (DcuS-DcuR two-component system) had some effect on dmlA expression. The anaerobic l -tartrate regulator TtdR or the oxygen sensors ArcB-ArcA and FNR did not have a m…

Physiology and MetabolismRegulatorMalatesDehydrogenasemedicine.disease_causeMicrobiologyMalate dehydrogenaseMicrobiologyMalate DehydrogenasemedicineAnaerobiosisMolecular BiologyEscherichia coliTartratesChromatography High Pressure LiquidbiologyEscherichia coli K12Escherichia coli ProteinsMetabolismGene Expression Regulation Bacterialbiology.organism_classificationbeta-GalactosidaseAerobiosisBiochemistryMutationFermentationAnaerobic exerciseBacteriaJournal of bacteriology
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Bacteriophage selection against a plasmid-encoded sex apparatus leads to the loss of antibiotic-resistance plasmids.

2011

Antibiotic-resistance genes are often carried by conjugative plasmids, which spread within and between bacterial species. It has long been recognized that some viruses of bacteria (bacteriophage; phage) have evolved to infect and kill plasmid-harbouring cells. This raises a question: can phages cause the loss of plasmid-associated antibiotic resistance by selecting for plasmid-free bacteria, or can bacteria or plasmids evolve resistance to phages in other ways? Here, we show that multiple antibiotic-resistance genes containing plasmids are stably maintained in bothEscherichia coliandSalmonella entericain the absence of phages, while plasmid-dependent phage PRD1 causes a dramatic reduction i…

Salmonella typhimuriumvirusesR Factorsmedicine.disease_causePolymerase Chain ReactionMicrobiologyBacteriophagePlasmidAntibiotic resistanceKanamycinDrug Resistance BacterialmedicineBacteriophage PRD1Selection GeneticEscherichia coliPhage typingGeneticsEvolutionary BiologybiologyEscherichia coli K12ta1182Kanamycinbiology.organism_classificationAgricultural and Biological Sciences (miscellaneous)Anti-Bacterial AgentsSalmonella entericaConjugation GeneticGenetic FitnessGeneral Agricultural and Biological SciencesBacteriamedicine.drugBiology Letters
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Efficient production of active chicken avidin using a bacterial signal peptide in Escherichia coli

2004

Chicken avidin is a highly popular tool with countless applications in the life sciences. In the present study, an efficient method for producing avidin protein in the periplasmic space of Escherichia coli in the active form is described. Avidin was produced by replacing the native signal sequence of the protein with a bacterial OmpA secretion signal. The yield after a single 2-iminobiotin–agarose affinity purification step was approx. 10 mg/l of virtually pure avidin. Purified avidin had 3.7 free biotin-binding sites per tetramer and showed the same biotin-binding affinity and thermal stability as egg-white avidin. Avidin crystallized under various conditions, which will enable X-ray cryst…

Signal peptideSpectrometry Mass Electrospray IonizationGlycosylationMolecular Sequence DataProtein Sorting Signalsmedicine.disease_causeBiochemistryAvian Proteinschemistry.chemical_compoundBacterial Proteinsstomatognathic systemTetramerAffinity chromatographymedicineAnimalsAmino Acid SequenceMolecular BiologyEscherichia coliEscherichia coli K12biologyCell BiologyPeriplasmic spacerespiratory systemAvidinMolecular WeightchemistryBiochemistryBiotinylationbiology.proteinChickensResearch ArticleBacterial Outer Membrane ProteinsAvidinBiochemical Journal
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Synergistic and Antagonistic Effects of Combined Subzero Temperature and High Pressure on Inactivation of Escherichia coli

2006

ABSTRACT The combined effects of subzero temperature and high pressure on the inactivation of Escherichia coli K12TG1 were investigated. Cells of this bacterial strain were exposed to high pressure (50 to 450 MPa, 10-min holding time) at two temperatures (−20°C without freezing and 25°C) and three water activity levels (a w ) (0.850, 0.992, and ca. 1.000) achieved with the addition of glycerol. There was a synergistic interaction between subzero temperature and high pressure in their effects on microbial inactivation. Indeed, to achieve the same inactivation rate, the pressures required at −20°C (in the liquid state) were more than 100 MPa less than those required at 25°C, at pressures in t…

Water activity[SDV]Life Sciences [q-bio]Hydrostatic pressureColony Count Microbialmedicine.disease_causeApplied Microbiology and BiotechnologySuspension (chemistry)03 medical and health scienceschemistry.chemical_compound[SPI]Engineering Sciences [physics]0404 agricultural biotechnologyAntimicrobial effectFreezingmedicineGlycerol[ SPI ] Engineering Sciences [physics]Hydrostatic PressureEscherichia coliComputingMilieux_MISCELLANEOUS0303 health sciencesEcology[ SDV ] Life Sciences [q-bio]Escherichia coli K12030306 microbiologyChemistryTemperatureWater04 agricultural and veterinary sciences040401 food scienceCulture MediaBiochemistryVolume (thermodynamics)High pressureBiophysicsFood MicrobiologyFood ScienceBiotechnology
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Polar Localization of a Tripartite Complex of the Two-Component System DcuS/DcuR and the Transporter DctA in Escherichia coli Depends on the Sensor K…

2014

The C4-dicarboxylate responsive sensor kinase DcuS of the DcuS/DcuR two-component system of E. coli is membrane-bound and reveals a polar localization. DcuS uses the C4-dicarboxylate transporter DctA as a co-regulator forming DctA/DcuS sensor units. Here it is shown by fluorescence microscopy with fusion proteins that DcuS has a dynamic and preferential polar localization, even at very low expression levels. Single assemblies of DcuS had high mobility in fast time lapse acquisitions, and fast recovery in FRAP experiments, excluding polar accumulation due to aggregation. DctA and DcuR fused to derivatives of the YFP protein are dispersed in the membrane or in the cytosol, respectively, when …

Yellow fluorescent proteinCardiolipinslcsh:MedicineMicrobiologyMreBMicrobial PhysiologyBacterial Physiologylcsh:ScienceCytoskeletonMicrobial MetabolismDicarboxylic Acid TransportersMultidisciplinaryEscherichia coli K12biologyBacterial GrowthEscherichia coli Proteinslcsh:RMicrobial Growth and DevelopmentBiology and Life SciencesFluorescence recovery after photobleachingBacteriologyFusion proteinTwo-component regulatory systemBacterial BiochemistryTransport proteinDNA-Binding ProteinsProtein TransportBiochemistryCytoplasmMultiprotein ComplexesBiophysicsbiology.proteinlcsh:QProtein KinasesResearch ArticleDevelopmental BiologyTranscription FactorsPLoS ONE
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