Search results for "(Escherichia coli)"

showing 10 items of 689 documents

DNA oxidation products determined with repair endonucleases in mammalian cells: Types, basal levels and influence of cell proliferation

1999

Purified repair endonucleases such as Fpg protein, endonuclease III and IV allow a very sensitive quantification of various types of oxidative DNA modifications in mammalian cells. By means of these assays, the numbers of base modifications sensitive to Fpg protein, which include 8-hydroxyguanine (8-oxoG), were determined to be less than 0.3 per 10(6) bp in several types of untreated cultured mammalian cells and human lymphocytes and less than 10 per 10(6) bp in mitochondrial DNA from rat and porcine liver. Oxidative 5,6-dihydropyrimidine derivatives sensitive to endonuclease III and sites of base loss sensitive to endonuclease IV or exonuclease III were much less frequent than Fpg-sensitiv…

DNA RepairBase pairDNA repairDNA damageCarbon-Oxygen LyasesCHO CellsDeferoxamineBiochemistryDeoxyribonuclease (Pyrimidine Dimer)chemistry.chemical_compoundCricetinaeDNA-(Apurinic or Apyrimidinic Site) LyaseAnimalsHumansDimethyl SulfoxideBase PairingN-Glycosyl HydrolasesChromatography High Pressure LiquidMammalsExonuclease IIIEndodeoxyribonucleasesPhotosensitizing AgentsGuanosinebiologyEscherichia coli ProteinsAcridine orangeDNAGeneral MedicineDNA oxidationOxidantsMolecular biologyDNA-(apurinic or apyrimidinic site) lyaseDeoxyribonuclease IV (Phage T4-Induced)DNA-Formamidopyrimidine GlycosylasechemistryBiochemistrybiology.proteinOxidation-ReductionCell DivisionDNAHeLa CellsFree Radical Research
researchProduct

Deinococcus radiodurans' SRA-HNH domain containing protein Shp (Dr1533) is involved in faithful genome inheritance maintenance following DNA damage

2018

WOS:000452343100012; International audience; Background: Deinococcus radiodurans R1 (DR) survives conditions of extreme desiccation, irradiation and exposure to genotoxic chemicals, due to efficient DNA breaks repair, also through Mn2+ protection of DNA repair enzymes. Methods: Possible annotated domains of the DR1533 locus protein (Shp) were searched by bioinformatic analysis. The gene was cloned and expressed as fusion protein. Band-shift assays of Shp or the SRA and HNH domains were performed on oligonucleotides, genomic DNA from E. coif and DR. slip knock-out mutant was generated by homologous recombination with a kanamycin resistance cassette. Results: DR1533 contains an N-terminal SRA…

DNA RepairDNA cytosine-methylation; DNA damage; DR1533 locus; Genotoxic agents; Mn2+; SRA domain; Biophysics; Biochemistry; Molecular BiologyGenotoxic agents[SDV]Life Sciences [q-bio]DNA cytosine-methylationperspectiveSettore BIO/19 - Microbiologia GeneraleBiochemistrychemistry.chemical_compound0302 clinical medicineKanamycinCloning Molecularcytosine0303 health sciencesDR1533 locusbiologyChemistryGenotoxic agentuhrf1Mn(2+)Mn2+SRA domainDeinococcusrecognitionmanganese(ii)DNA BacterialDNA damageDNA repairoxidationUbiquitin-Protein LigasesBiophysicsSettore BIO/11 - Biologia Molecolareresistance03 medical and health sciencesBacterial ProteinsProtein DomainsDR1533 locuDrug Resistance BacterialEscherichia coliHumansfeaturesAmino Acid SequenceGeneMolecular Biology030304 developmental biologyOligonucleotideComputational BiologyDeinococcus radioduransDNA Methylationbiology.organism_classificationMolecular biologygenomic DNArepairMutationCCAAT-Enhancer-Binding ProteinsDNA damageHomologous recombination030217 neurology & neurosurgeryDNAGenome BacterialMutagens
researchProduct

Purification of Leuconostoc mesenteroides citrate lyase and cloning and characterization of the citCDEFG gene cluster

1998

ABSTRACT A citrate lyase (EC 4.1.3.6 ) was purified 25-fold from Leuconostoc mesenteroides and was shown to contain three subunits. The first 42 amino acids of the β subunit were identified, as well as an internal peptide sequence spanning some 20 amino acids into the α subunit. Using degenerated primers from these sequences, we amplified a 1.2-kb DNA fragment by PCR from Leuconostoc mesenteroides subsp. cremoris . This fragment was used as a probe for screening a Leuconostoc genomic bank to identify the structural genes. The 2.7-kb gene cluster encoding citrate lyase of L. mesenteroides is organized in three open reading frames, citD , citE , and citF , encoding, respectively, the three ci…

DNA BacterialATP citrate lyaseMolecular Sequence DataGene ExpressionBiologymedicine.disease_causeMicrobiologyBacterial ProteinsCarbon-Sulfur LigasesMultienzyme ComplexesGene clusterAcyl Carrier ProteinEscherichia colimedicineLeuconostocAmino Acid SequenceCloning MolecularMolecular BiologyEscherichia coliBase SequenceSequence Homology Amino AcidStructural geneOxo-Acid-LyasesSequence Analysis DNALyasebiology.organism_classificationEnzymes and ProteinsMolecular biologyOxaloacetate decarboxylaseBiochemistryGenes BacterialLeuconostoc mesenteroidesMultigene FamilyCoenzyme A-TransferasesLeuconostoc
researchProduct

A Sensitive Method for Identification of DNA Dependent DNA Polymerases in Acrylamide Gels after Seperation by Micro Disc Electrophoresis

1973

Abstract DNA polymerase, disc electrophoresis, template affinity Two sensitive methods are described for detection of DNA dependent DNA polymerase activities in polyacrylamide gels after their fractionation by micro-disc electrophoresis. One technique is based on the increase in fluorescence of the ethidium bromide complex with template polydeoxyribonucleotides brought about by the action of the polymerases. The sensitivity of the previously described technique has been enhanced. Another method, 14 fold as sensitive, uses radioactive precursors in the enzyme assay after electrophoretic separation; washing, slicing and counting allows to evaluate incorporation into acid insoluble polymer, re…

DNA BacterialAcrylamidesbiologyDNA polymeraseElectrophoresis DiscTritiummedicine.disease_causeFluorescenceGeneral Biochemistry Genetics and Molecular Biologychemistry.chemical_compoundBiochemistrychemistryDisc electrophoresisEthidiumAcrylamideDNA NucleotidyltransferasesEscherichia coliMethodsbiology.proteinmedicineGelsEscherichia coliDNA-directed DNA polymeraseDensitometryDNA NucleotidyltransferasesZeitschrift für Naturforschung C
researchProduct

Impact of biocide treatments on the bacterial communities of the Lascaux Cave.

2009

The Lascaux Cave contains a remarkable set of paintings from the Upper Palaeolithic. Shortly after discovery in 1940, the cave was modified for public viewing and, in 2001, was invaded by a Fusarium solani species complex. Benzalkonium chloride was used from 2001 to 2004 to eliminate the fungal outbreak. In this study, we carried out a sampling in most of the cave halls and galleries. Sequence analysis and isolation methods detected that the most abundant genera of bacteria were Ralstonia and Pseudomonas. We suggest that, as a result of years of benzalkonium chloride treatments, the indigenous microbial community has been replaced by microbial populations selected by biocide application.

DNA BacterialBiocideGeologic SedimentsLegionellaRalstonia03 medical and health sciencesBenzalkonium chlorideBENZALKONIUM CHLORIDERalstoniaCaveLASCAUX CAVEPseudomonasBotanymedicineEscherichia coliAlcaligenesDNA FungalEcology Evolution Behavior and Systematics030304 developmental biology[SDV.EE]Life Sciences [q-bio]/Ecology environment0303 health sciencesgeographygeography.geographical_feature_categoryBenzalkonium chloride . Ralstonia spp. . Pseudomonas spp. . Lascaux Cavebiology030306 microbiologyEcologyFungal geneticsFungiOutbreakGeneral Medicinebiology.organism_classificationIsolation (microbiology)[SDV.MP.BAC]Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyhumanitiesMicrobial population biologyPaintingsFrance[SDV.MP.BAC] Life Sciences [q-bio]/Microbiology and Parasitology/BacteriologyRALSTONIA SPP.Benzalkonium Compoundsmedicine.drugDisinfectantsDie Naturwissenschaften
researchProduct

Gene Cloning, Transcriptional Analysis, Purification, and Characterization of Phenolic Acid Decarboxylase from Bacillus subtilis

1998

Phenolic acids, also called substituted cinnamic acids, are important lignin-related aromatic acids and natural constituents of plant cell walls. These acids (particularly ferulic, p-coumaric, and caffeic acids) bind the complex lignin polymer to the hemicellulose and cellulose in plants (1) or are generally esterified with tartaric acid (for example, in grape must, wine, and cider) and can be released as free acids during wine making by some cinnamoyl esterase activities (9). Most often, free phenolic acids are metabolized by different microorganisms into 4-vinyl derivatives and then are eventually reduced into 4-ethyl derivatives (5, 6). Some of these volatile phenols, particularly vinyl …

DNA BacterialCarboxy-lyasesCarboxy-LyasesMolecular Sequence DataGenetics and Molecular BiologyBacillus subtilisBiologyApplied Microbiology and BiotechnologyEsteraseGene Expression Regulation EnzymologicSubstrate SpecificityFerulic acidchemistry.chemical_compoundCaffeic acidEscherichia coliPhenolsAmino Acid SequenceCloning MolecularDNA Primerschemistry.chemical_classificationEcologyBase SequenceSequence Homology Amino Acidfood and beveragesChromosome MappingPhenolic acidGene Expression Regulation Bacterialbiology.organism_classificationRecombinant ProteinsAmino acidchemistryBiochemistryGenes BacterialbacteriaFood ScienceBiotechnologyBacillus subtilis
researchProduct

Mutational Events in Cefotaximase Extended-Spectrum β-Lactamases of the CTX-M-1 Cluster Involved in Ceftazidime Resistance

2008

ABSTRACT CTX-M β-lactamases, which show a high cefotaxime hydrolytic activity, constitute the most prevalent extended-spectrum β-lactamase (ESBL) type found among clinical isolates. The recent explosive diversification of CTX-M enzymes seems to have taken place due to the appearance of more efficient enzymes which are capable of hydrolyzing both cefotaxime and ceftazidime, especially among the CTX-M-1 cluster. A combined strategy of in vitro stepwise evolution experiments using bla CTX-M-1 , bla CTX-M-3 , and bla CTX-M-10 genes and site-directed mutagenesis has been used to evaluate the role of ceftazidime and other β-lactam antibiotics in triggering the diversity found among enzymes belong…

DNA BacterialCefotaximeCefepimeCeftazidimeMutagenesis (molecular biology technique)Context (language use)CefotaximeBiologymedicine.disease_causeCeftazidimebeta-LactamasesMicrobiologyEvolution MolecularMechanisms of ResistanceEscherichia colimedicineHumansPharmacology (medical)DNA PrimersCephalosporin ResistanceAntibacterial agentPharmacologyGeneticsMutationBase SequenceCephalosporin ResistanceGenetic VariationAnti-Bacterial AgentsPhenotypeInfectious DiseasesGenes BacterialMultigene FamilyMutationMutagenesis Site-Directedmedicine.drugAntimicrobial Agents and Chemotherapy
researchProduct

Expression in Streptomyces lividans of Nonomuraea genes cloned in an artificial chromosome

2004

A bacterial artificial chromosomal library of Nonomuraea sp. ATCC39727 was constructed using Escherichia coli-Streptomyces artificial chromosome (ESAC) and screened for the presence of dbv genes known to be involved in the biosynthesis of the glycopeptide A40926. dbv genes were cloned as two large, partially overlapping, fragments and transferred into the host Streptomyces lividans, thus generating strains S. lividansColon, two colonsNmESAC50 and S. lividansColon, two colonsNmESAC57. The heterologous expression of Nonomuraea genes in S. lividans was successfully demonstrated by using combined RT-PCR and proteomic approaches. MALDI-TOF analysis revealed that a Nonomuraea ABC transporter is e…

DNA BacterialChromosomal library of Nonomuraea sp. ATCC39727Escherichia coli–Streptomyces artificial chromosome (ESAC)RT-PCRMolecular cloningApplied Microbiology and BiotechnologyStreptomycesGenetic analysisThiostreptonchemistry.chemical_compoundActinomycetalesChromosomes ArtificialCloning MolecularA40926GeneRegulator geneGeneticsGenomic LibrarybiologyMALDI-TOF mass spectrometryPromoterGeneral Medicinebiology.organism_classificationStreptomycesdbv gene cluster2D-PAGEchemistryGenes BacterialHeterologous expressionHeterologous expressionPulsed field gel electrophoresidalbavancinBiotechnologyApplied Microbiology and Biotechnology
researchProduct

Cloning, deletion, and characterization of PadR, the transcriptional repressor of the phenolic acid decarboxylase-encoding padA gene of Lactobacillus…

2004

ABSTRACTLactobacillus plantarumdisplays a substrate-induciblepadAgene encoding a phenolic acid decarboxylase enzyme (PadA) that is considered a specific chemical stress response to the inducing substrate. The putative regulator ofpadAwas located in thepadAlocus based on its 52% identity with PadR, thepadAgene transcriptional regulator ofPediococcus pentosaceus(L. Barthelmebs, B. Lecomte, C. Diviès, and J.-F. Cavin, J. Bacteriol.182:6724-6731, 2000). Deletion of theL. plantarum padRgene clearly demonstrates that the protein it encodes is the transcriptional repressor of divergently orientedpadA. ThepadRgene is cotranscribed with a downstream open reading frame (ORF1), the product of which m…

DNA BacterialCoumaric AcidsCarboxy-LyasesMolecular Sequence DataRepressorGenetics and Molecular BiologyBiologymedicine.disease_causeApplied Microbiology and BiotechnologyOpen Reading FramesBacterial ProteinsTranscription (biology)Transcriptional regulationmedicineAmino Acid SequenceCloning MolecularPromoter Regions GeneticGeneEscherichia coliDNA PrimersBinding SitesEcologyBase SequenceSequence Homology Amino Acidfood and beveragesPromoterbiology.organism_classificationMolecular biologyRepressor ProteinsOpen reading frameLactobacillusBiochemistryGenes BacterialPropionatesLactobacillus plantarumGene DeletionFood ScienceBiotechnologyApplied and environmental microbiology
researchProduct

Domain organization and evolution of multifunctional autoprocessing repeats-in-toxin (MARTX) toxin in Vibrio vulnificus.

2011

ABSTRACT The objective of this study was to analyze multifunctional autoprocessing repeats-in-toxin (MARTX) toxin domain organization within the aquatic species Vibrio vulnificus as well as to study the evolution of the rtxA1 gene. The species is subdivided into three biotypes that differ in host range and geographical distribution. We have found three different types (I, II, and III) of V. vulnificus MARTX (MARTX Vv ) toxins with common domains (an autocatalytic cysteine protease domain [CPD], an α / β-hydrolase domain, and a domain resembling that of the LifA protein of Escherichia coli O127:H6 E2348/69 [Efa/LifA]) and specific domains (a Rho-GTPase inactivation domain [RID], a domain of …

DNA BacterialGene Transfer HorizontalBacterial ToxinsMolecular Sequence DataVibrio vulnificusmedicine.disease_causeApplied Microbiology and BiotechnologyBacterisMicrobiologyEvolution MolecularVibrionaceaemedicineEvolutionary and Genomic MicrobiologyVibrio vulnificusGeneEscherichia coliGenètica bacterianaGeographyEcologybiologyToxinSequence Analysis DNAbiology.organism_classificationCysteine proteaseBacterial Typing TechniquesProtein Structure TertiaryHorizontal gene transferBacteris patògensBacteriaFood ScienceBiotechnology
researchProduct