Search results for "Erich"

showing 10 items of 805 documents

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
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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
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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
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The Evolutionary Fate of Nonfunctional DNA in the Bacterial Endosymbiont Buchnera aphidicola

2004

Reduction of the genome size in endosymbiotic bacteria is the main feature linked to the adaptation to a host-associated lifestyle. We have analyzed the fate of the nonfunctional DNA in Buchnera aphidicola, the primary endosymbiont of aphids. At least 164 gene losses took place during the recent evolution of three B. aphidicola strains, symbionts of the aphids Acyrthosiphon pisum (BAp), Schizaphis graminum (BSg), and Baizongia pistacia (BBp). A typical pattern starts with the inactivation of a gene, which produces a pseudogene, and is followed by the progressive loss of its DNA. Our results show that during the period from the separation of the Aphidinae and Pemphiginae lineages (86-164 MYA…

DNA BacterialGeneticsTime FactorsModels GeneticPseudogenemyrDNASequence Analysis DNABiologybiology.organism_classificationGenomeEvolution MolecularIntergenic regionBuchneraSpecies SpecificityEscherichia coliGeneticsBuchneraMolecular BiologyGeneGenome sizeGene DeletionGenome BacterialEcology Evolution Behavior and SystematicsGC-contentMolecular Biology and Evolution
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Mutagenicity test system based on a reporter gene assay for short-term detection of mutagens (MutaGen assay).

2003

Abstract The construction of a bacterial mutation assay system detecting reversions of base substitutions and frameshifts in tetracycline (tet) and ampicillin resistance genes located on low copy plasmids is described. Frameshift mutations were introduced into repetitive GC-sequences and G-repeats known to be mutagenic hot-spots. Base pair substitutions were inserted in or around the active site of the ampicillinase gene thus generating reversibility of the ampicilline sensitivity. The plasmids carry genes to enable sensitive, fast and specific detection of mutagens in bacteria. MucAB was cloned into the test plasmid to enhance error-prone DNA-repair. The conventional reversion principle ha…

DNA BacterialHealth Toxicology and MutagenesisMolecular Sequence DataMutagenBiologymedicine.disease_causeFrameshift mutationchemistry.chemical_compoundPlasmidAmp resistanceGenes ReporterGeneticsmedicineEscherichia coliPoint MutationAmino Acid SequenceFrameshift MutationGeneMutationReporter geneBase SequenceMutagenicity TestsTetracycline ResistanceMolecular biologychemistryLac OperonMutagenesis Site-DirectedDNAAmpicillin ResistanceMutagensPlasmidsMutation research
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Growth phase-dependent regulation of nuoA-N expression in Escherichia coli K-12 by the Fis protein: upstream binding sites and bioenergetic significa…

2000

The expression of the nuoA-N operon of Escherichia coli K-12, which encodes the proton-pumping NADH dehydrogenase I is modulated by growth phase-dependent regulation. Under respiratory growth conditions, expression was stimulated in early exponential, and to a lesser extent in late exponential and stationary growth phases. The stimulation in the early exponential growth phase was not observed in fis mutants, which are deficient for the growth phase-responsive regulator Fis. Neither the alternative sigma factor RpoS nor the integration host factor (IHF) are involved in growth phase-dependent regulation of this operon. When incubated with nuo promoter DNA, isolated Fis protein formed three re…

DNA BacterialIntegration Host FactorsOperonMutantMolecular Sequence DataBiologymedicine.disease_causeExponential growthBacterial ProteinsFactor For Inversion Stimulation ProteinOperonGeneticsmedicineEscherichia coliBinding sitePromoter Regions GeneticMolecular BiologyEscherichia coliBinding SitesBase SequenceEscherichia coli ProteinsDNase-I FootprintingPromoterMolecular biologyCarrier ProteinsrpoSMoleculargeneral genetics : MGG
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Cloning and characterization of the genes encoding the malolactic enzyme and the malate permease of Leuconostoc oenos

1996

Using degenerated primers from conserved regions of the protein sequences of malic enzymes, we amplified a 324-bp DNA fragment by PCR from Leuconostoc oenos and used this fragment as a probe for screening a Leuconostoc oenos genomic bank. Of the 2,990 clones in the genomic bank examined, 7 with overlapping fragments were isolated by performing colony hybridization experiments. Sequencing 3,453 bp from overlapping fragments revealed two open reading frames that were 1,623 and 942 nucleotides long and were followed by a putative terminator structure. The first deduced protein (molecular weight, 59,118) is very similar (level of similarity, 66%) to the malolactic enzyme of Lactococcus lactis; …

DNA BacterialMalolactic enzymeLeuconostoc oenosMolecular Sequence DataRestriction MappingMalatesBiological Transport ActiveOrganic Anion TransportersSaccharomyces cerevisiaeBiologyPolymerase Chain ReactionApplied Microbiology and BiotechnologyMalate dehydrogenaseOpen Reading FramesBacterial ProteinsMalate DehydrogenaseGene cluster[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyEscherichia coliLeuconostocAmino Acid SequenceCloning MolecularMalate transportDNA PrimersGenomic organizationBase SequenceSequence Homology Amino AcidEcologyLactococcus lactisNucleic acid sequenceMembrane Transport Proteinsbiology.organism_classificationMolecular biologymalate permeaseMolecular WeightOpen reading frameBiochemistryGenes BacterialLeuconostocResearch ArticleFood ScienceBiotechnologyApplied and Environmental Microbiology
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Identification of a clone of Escherichia coli O103:H2 as a potential agent of hemolytic-uremic syndrome in France

1993

In a French multicenter study, six verocytotoxin-producing Escherichia coli strains were isolated from the stools of 6 of 69 children suffering from hemolytic-uremic syndrome. All strains belonged to serotype O103:H2, a serotype commonly associated with diarrhea in weaned rabbits in France. To determine whether the strains from humans and rabbits were genetically related, they were compared by analyzing their esterase electropherotypes and the restriction fragment length polymorphisms of the ribosomal DNA regions. A common clonal origin of these pathogenic strains was suggested by their identical esterase electropherotypes and their identical ribotypes, in addition to their identical seroty…

DNA BacterialMicrobiology (medical)SerotypeBacterial ToxinsMolecular Sequence DataClone (cell biology)VirulenceVerocytotoxinShiga Toxin 1medicine.disease_causePolymerase Chain Reactionlaw.inventionMicrobiology03 medical and health scienceschemistry.chemical_compoundlawEscherichia colimedicineHumansSerotyping[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyEscherichia coliEscherichia coli InfectionsComputingMilieux_MISCELLANEOUSPolymerase chain reaction030304 developmental biology0303 health sciencesBase SequenceVirulencebiology030306 microbiologyInfantCorrectionbiology.organism_classificationEnterobacteriaceae3. Good healthBacterial adhesinPOUVOIR PATHOGENE[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologychemistryChild PreschoolHemolytic-Uremic SyndromeFranceResearch ArticleJournal of Clinical Microbiology
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An electrochemical DNA biosensor for the detection of CTX-M extended-spectrum β-lactamase-producing Escherichia coli in soil samples

2013

International audience; An electrochemical hybridization assay involving neutravidin-coated carbon screen-printed electrodes and an HRP-based detection have been shown to provide an effective tool for the genotypic analysis of extended-spectrum beta-lactamase-producing E. coli strains in complex samples such as soil. (c) 2012 Elsevier B.V. All rights reserved.

DNA BacterialMicrobiology (medical)Soil test[SDV]Life Sciences [q-bio]Biosensing TechniquesBiologymedicine.disease_causeElectrochemistry01 natural sciencesMicrobiologybeta-LactamasesMicrobiologySoil03 medical and health scienceschemistry.chemical_compoundEscherichia colimedicine[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyCTX-MScreen-printed carbon electrodesMolecular BiologyEscherichia coliSoil Microbiology0303 health sciencesChromatographyIDENTIFICATION030306 microbiology010401 analytical chemistryE. coliElectrochemical TechniquesExtended-spectrum beta-lactamase0104 chemical scienceschemistry[SDE]Environmental SciencesBiosensorSoil microbiologyDNA biosensorDNAJournal of Microbiological Methods
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Cloning and sequencing of the dnaK region of Streptomyces coelicolor A3(2)

1993

Abstract The dnaK homologue of Streptomyces coelicolor A3(2) strain M145 has been cloned and sequenced. Nucleotide sequence analysis of a 2.5-kb region revealed an open reading frame (ORF) encoding a predicted DnaK protein of 618 amino acids (Mr = 66 274). The dnaK coding sequence displays extreme codon bias and shows a strong preference for CGY and GGY, for Arg and Gly codons, respectively. The predicted DnaK sequence has a high Lys:Arg ratio which is not typical of streptomycete proteins. The region immediately downstream from dnaK contains an ORF for a GrpE-like protein; the predicted start codon of grpE overlaps the last two codons of dnaK, indicating that the two genes are translationa…

DNA BacterialMolecular Sequence Datagenetic processesBacterial ProteinsStart codonGeneticsCoding regionHSP70 Heat-Shock ProteinsAmino Acid SequenceCloning MolecularCodonGeneHeat-Shock Proteinschemistry.chemical_classificationGeneticsBase SequencebiologyEscherichia coli ProteinsStreptomyces coelicolorNucleic acid sequenceStreptococcusGeneral Medicinebiology.organism_classificationAmino acidOpen reading framechemistryGenes BacterialProtein BiosynthesisCodon usage biasbiological sciencesbacteriaSequence AlignmentGene
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