Search results for "ESCHERICHIA COLI"

showing 10 items of 689 documents

Construction and expression of a dual vector for chemo-enzymatic synthesis of plant indole alkaloids inEscherichia coli

2010

A dual vector (pQE-70-STR1-SG) containing coding regions of strictosidine synthase (STR1, EC 4.3.3.2) and strictosidine glucosidase (SG, EC 3.2.1.105) from the Indian medicinal plant Rauvolfia serpentina was constructed. Functional expression of the vector in Escherichia coli cells (M15 strain) was proven by isolation of prepurified enzyme extracts, which show both STR1 and SG activities. Incubation of the enzyme in the presence of tryptamine and secologanin delivered the indole alkaloid cathenamine, demonstrating functional co-expression of both STR1- and SG-cDNAs. Cathenamine reduction by sodium borohydride leading to tetrahydroalstonine revealed the chemo-enzymatic indole alkaloid synthe…

TryptamineDNA ComplementaryStrictosidine synthasePlant Sciencemedicine.disease_causeBiochemistryGene Expression Regulation EnzymologicRauwolfiaIndole AlkaloidsAnalytical Chemistrychemistry.chemical_compoundGene Expression Regulation PlantRauvolfia serpentinaCarbon-Nitrogen LyasesEscherichia colimedicineCloning MolecularEscherichia coliPlant ProteinsIndole testchemistry.chemical_classificationMolecular StructurebiologyIndole alkaloidOrganic Chemistrybiology.organism_classificationSecologanin Tryptamine AlkaloidsEnzymechemistryBiochemistrybiology.proteinSecologaninGlucosidasesNatural Product Research
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Determination of enrichment factors for modified RNA in MeRIP experiments

2019

In the growing field of RNA modification, precipitation techniques using antibodies play an important role. However, little is known about their specificities and protocols are missing to assess their effectiveness. Here we present a method to assess enrichment factors after MeRIP-type pulldown experiments, here exemplified with a commercial antibody against N6-methyladenosine (m6A). Testing different pulldown and elution conditions, we measure enrichment factors of 4-5 using m6A-containing mRNAs against an unmodified control of identical sequence. Both types of mRNA carry 32P labels at different nucleotides, allowing their relative quantification in a mixture after digestion to nucleotides…

Models MolecularAdenosineAbsolute quantificationMethylationProtein Structure SecondaryGeneral Biochemistry Genetics and Molecular BiologyViral Proteins03 medical and health sciencesAdenosine TriphosphateRNA modificationEscherichia coliHumansImmunoprecipitationProtein Interaction Domains and MotifsNucleotideRNA MessengerMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesMessenger RNACell-Free SystemChemistryElution030302 biochemistry & molecular biologyRNADNA-Directed RNA PolymerasesBiochemistryImmunoglobulin GIsotope LabelingChromatography Thin LayerPhosphorus RadioisotopesProtein BindingMethods
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Diversity and Evolution of the Phenazine Biosynthesis Pathway

2010

ABSTRACT Phenazines are versatile secondary metabolites of bacterial origin that function in biological control of plant pathogens and contribute to the ecological fitness and pathogenicity of the producing strains. In this study, we employed a collection of 94 strains having various geographic, environmental, and clinical origins to study the distribution and evolution of phenazine genes in members of the genera Pseudomonas , Burkholderia , Pectobacterium , Brevibacterium , and Streptomyces . Our results confirmed the diversity of phenazine producers and revealed that most of them appear to be soil-dwelling and/or plant-associated species. Genome analyses and comparisons of phylogenies inf…

Antifungal Agentsgenome sequenceaeruginosa pao1virulence factorsphenazine-1-carboxylic acidVIRULENCE FACTORS GENE-CLUSTERApplied Microbiology and Biotechnologychemistry.chemical_compoundGene clusterEnvironmental MicrobiologyPhylogenySoil Microbiologyfluorescent pseudomonas2. Zero hungerGenetics0303 health sciencesEcologybiologyEPS-2PseudomonasPlants[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyMultigene FamilyHorizontal gene transferBiotechnologyDNA BacterialWashingtonPectobacteriumGene Transfer HorizontalGenotypeSequence analysisMolecular Sequence DataPhenazineerwinia-herbicola eh1087pseudomonas-chlororaphis pcl1391Evolution Molecular03 medical and health sciencesBacterial ProteinsPseudomonasBotanyEscherichia coli030304 developmental biologyBacteriaBase SequencePSEUDOMONAS-CHLORORAPHIS030306 microbiologybiological-controlGene Expression Regulation BacterialSequence Analysis DNA15. Life on landbiology.organism_classificationrpoBERWINIA-HERBICOLAPHENAZINEBiosynthetic Pathwaysgene-clusterLaboratorium voor PhytopathologieBurkholderiachemistryGenes BacterialLaboratory of PhytopathologyPhenazinesburkholderia-cepacia complexSequence AlignmentFood Science
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GTPases of the Rho Subfamily Are Required for Brucella abortus Internalization in Nonprofessional Phagocytes

2001

Members of the genus Brucella are intracellular -Proteobacteria responsible for brucellosis, a chronic disease of humans and animals. Little is known about Brucella virulence mechanisms, but the abilities of these bacteria to invade and to survive within cells are decisive factors for causing disease. Transmission electron and fluorescence microscopy of infected nonprofessional phagocytic HeLa cells revealed minor membrane changes accompanied by discrete recruitment of F-actin at the site of Brucella abortus entry. Cell uptake of B. abortus was negatively affected to various degrees by actin, actin-myosin, and microtubule chemical inhibitors. Modulators of MAPKs and protein-tyrosine kinases…

biologymedia_common.quotation_subjectIntracellular parasiteBRUCELLA ABORTUSVirulenceCell BiologyCDC42BrucellaGTPasebiology.organism_classificationBiochemistryMicrobiologyBRUCELOSISCytotoxic T cellBRUCELLAESCHERICHIA COLIBACTERIASInternalizationMolecular BiologyIntracellularmedia_commonJournal of Biological Chemistry
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H89 Treatment Reduces Intestinal Inflammation and Candida albicans Overgrowth in Mice

2020

Deregulation of the dynamic crosstalk between the gut microbiota, intestinal epithelial cells, and immune cells is critically involved in the development of inflammatory bowel disease and the overgrowth of opportunistic pathogens, including the human opportunistic fungus Candida albicans. In the present study, we assessed the effect of N-[2-(p-bromocinnamylamino)ethyl]-5-isoquinolinesulfonamide (H89), a protein kinase A inhibitor, on the migration of macrophages to C. albicans through dextran sulphate sodium (DSS)-challenged Caco-2 cells. We also investigated the impact of H89 on intestinal inflammation and C. albicans clearance from the gut, and determined the diversity of the gut microbio…

0301 basic medicineMicrobiology (medical)<i>Lactobacillus johnsonii</i>colitisH89030106 microbiologyInflammationGut floraMicrobiologydigestive systemArticleMicrobiology03 medical and health sciences<i>Enterococcus faecalis</i>Immune system[SDV.MHEP.MI]Life Sciences [q-bio]/Human health and pathology/Infectious diseasesVirologyCandida albicansmedicineEscherichia coliEnterococcus faecalismicrobiotaColitisCandida albicanslcsh:QH301-705.5Lactobacillus johnsoniiLactobacillus johnsoniiDSSH89;Candida albicans;Escherichia coli;Enterococcus faecalis;Lactobacillus johnsonii;microbiota;DSS;colitis;protein kinase AInnate immune systembiology<i>Escherichia coli</i>[SDV.MHEP.HEG]Life Sciences [q-bio]/Human health and pathology/Hépatology and Gastroenterologymedicine.diseasebiology.organism_classificationCorpus albicans3. Good health<i>Candida albicans</i>030104 developmental biologylcsh:Biology (General)[SDV.SP.PHARMA]Life Sciences [q-bio]/Pharmaceutical sciences/Pharmacologyprotein kinase Amedicine.symptomMicroorganisms
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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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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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A rhamnose-binding lectin from sea bass (Dicentrarchus labrax) plasma agglutinates and opsonizes pathogenic bacteria

2014

Abstract The discovery of rhamnose-binding lectins (RBLs) in teleost fish eggs led to the identification of a novel lectin family characterized by a unique sequence motif and a structural fold, and initially proposed to modulate fertilization. Further studies of the RBL tissue localization and gene organization were also suggestive of role(s) in innate immunity. Here we describe the purification, and biochemical and functional characterization of a novel RBL (DlRBL) from sea bass (Dicentrarchus labrax) serum. The purified DlRBL had electrophoretic mobilities corresponding to 24 kDa and 100 kDa under reducing and non-reducing conditions, respectively, suggesting that in plasma the DlRBL is p…

AgglutinationGram-negative bacteriaErythrocytesRhamnoselectin; D. labraxImmunologyAmino Acid MotifsMolecular Sequence DataRhamnoseArticlechemistry.chemical_compoundPlasmaPhagocytosisLectinsEscherichia coliAnimalsAmino Acid SequenceSea bassPeptide sequencePhylogenybiologyD. labraxLectinRhamnose bindingBacterial Infectionsbiology.organism_classificationImmunity InnateProtein Structure TertiaryBiochemistrychemistrybiology.proteinMacrophages PeritoneallectinBassRabbitsProtein MultimerizationSequence motifDevelopmental BiologyHomotetramerProtein Binding
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Comparison of necrotoxigenic Escherichia coli isolates from farm animals and from humans.

1999

Abstract Necrotoxigenic Escherichia coli (NTEC) isolated from animals and humans can belong to the same serogroups/types and produce or carry the genes coding for fimbrial and afimbrial adhesins of the same family, P, S, F17, and/or AFA, raising the question of a potential zoonotic source of human infection. The main purpose of this study was to compare 239 NTEC1 strains (45 from cattle, 65 from humans and 129 from piglets) and 98 NTEC2 strains from cattle, using a uniform and standardized typing scheme. The O serogroups and the biotypes recognized amongst NTEC1 and NTEC2 strains were quite varied, although some were more frequently observed (serogroups O2, O4, O6, O8, O18, O78, and O83 and…

GenotypeSwine[SDV]Life Sciences [q-bio]Biologymedicine.disease_causeMicrobiologyMicrobiologychemistry.chemical_compoundHemolysin ProteinsGenotypemedicineEscherichia coliAnimalsHumansTypingSerotypingEscherichia coliGeneral VeterinaryHemolysinGeneral Medicinebiology.organism_classificationEnterobacteriaceaeBacterial adhesin[SDV] Life Sciences [q-bio]PhenotypechemistryColicinAerobactinCattleVeterinary microbiology
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Structural insights into the GTPase domain of Escherichia coli MnmE protein

2007

The Escherichia coli MnmE protein is a 50-kDa multidomain GTPase involved in tRNA modification. Its homologues in eukaryotes are crucial for mitochondrial respiration and, thus, it is thought that the human protein might be involved in mitochondrial diseases. Unlike Ras, MnmE shows a high intrinsic GTPase activity and requires effective GTP hydrolysis, and not simply GTP binding, to be functionally active. The isolated MnmE G-domain (165 residues) conserves the GTPase activity of the entire protein, suggesting that it contains the catalytic residues for GTP hydrolysis. To explore the GTP hydrolysis mechanism of MnmE, we analyzed the effect of low pH on binding and hydrolysis of GTP, as well…

Models MolecularTRNA modificationMagnetic Resonance SpectroscopyGTP'aluminium fluoridehomology modelingMolecular Sequence DataGTPaseGuanosine triphosphateGuanosine DiphosphateBiochemistryeraGTP Phosphohydrolaseschemistry.chemical_compoundStructural BiologyEscherichia coliAmino Acid SequenceHomology modelingBinding siteGTPaseMolecular BiologyBinding SitesSequence Homology Amino AcidChemistryEscherichia coli ProteinsTrmENMRRecombinant ProteinsKineticsBiochemistryMnmEGuanosine diphosphateRap2AGTP PhosphohydrolasesGuanosine TriphosphateSequence AlignmentRasProteins: Structure, Function, and Bioinformatics
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