Search results for "Cloning"

showing 10 items of 498 documents

EGFP Reporters for Direct and Sensitive Detection of Mutagenic Bypass of DNA Lesions

2020

The sustainment of replication and transcription of damaged DNA is essential for cell survival under genotoxic stress

DNA RepairTranscription GeneticDNA damageMutantGenetic VectorsGreen Fluorescent Proteinslcsh:QR1-502host cell reactivation (HCR)BiochemistryArticlelcsh:Microbiology03 medical and health scienceschemistry.chemical_compoundmutation assay0302 clinical medicinetranslesion synthesis (TLS)transcriptional mutagenesisTranscription (biology)Genes ReporterHumansCloning MolecularMolecular Biologyenhanced green fluorescent protein (EGFP)PolymeraseCells CulturedDNA damage tolerance030304 developmental biology0303 health sciencesbiologyDNA synthesisChemistryPoint mutationreporter assayRNACell biologyAmino Acid SubstitutionMutagenesis030220 oncology & carcinogenesisMutationbiology.proteinDNA damageDNAHeLa Cellsdamage bypassBiomolecules
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Origin of the integrin-mediated signal transduction. Functional studies with cell cultures from the sponge Suberites domuncula

1999

Sponges (phylum Porifera) represent the phylogenetically oldest metazoan animals. Recently, from the marine sponge Geodia cydonium a first cDNA encoding a putative integrin receptor molecule was isolated. In the present study basic functional experiments have been conducted to test the hypothesis that in sponges integrin polypeptides also function as adhesion molecules and as outside-in signaling molecules. The sponge Suberites domuncula has been used for the experiments because from this sponge only has a cell culture been established. Here we report that aggregation factor (AF)-mediated cell-cell adhesion is blocked by the RGDS peptide which is known to interact with beta integrin. Both R…

DNA ReplicationIntegrinsMolecular Sequence DataIntegrinBiologyBiochemistryCD49cEvolution MolecularCalmodulinCell AdhesionAnimalsAmino Acid SequenceRNA MessengerCloning MolecularCell adhesionCells CulturedCell AggregationCell adhesion moleculeSequence Analysis DNAbiology.organism_classificationCell aggregationPoriferaCell biologysuberites domuncula; integrin; calcium; ras; calmodulin; signal transduction; evolution; rgd(s)Suberites domunculaGene Expression RegulationIntegrin alpha Mras Proteinsbiology.proteinCalciumIntegrin beta 6Cell Adhesion MoleculesOligopeptidesSignal TransductionEuropean Journal of Biochemistry
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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
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Cloning and sequencing of the gene encoding α-acetolactate decarboxylase fromLeuconostoc oenos

1996

The alsD gene encoding alpha-acetolactate decarboxylase was isolated from a genomic library of Leuconostoc oenos, using a screening procedure developed on microtiter plates. The nucleotide sequence of alsD encodes a putative protein of 239 amino acids showing significant similarity with other bacterial alpha-acetolactate decarboxylases. Upstream from alsD lies an open reading frame (alsS) which is highly similar to bacterial genes coding for catabolic alpha-acetolactate synthases. Northern (RNA) blotting analyses indicated the presence of a 2.4-kb dicistronic transcript of alsS and alsD. This suggests that the alsS and alsD genes are organized in a single operon.

DNA BacterialCarboxy-LyasesOperonMolecular Sequence DataRestriction MappingBiologyMicrobiologyGene Expression Regulation EnzymologicGeneticsLeuconostocGenomic libraryCloning MolecularMolecular BiologyGeneGeneticsCloningSequence Homology Amino AcidNucleic acid sequenceGene Expression Regulation BacterialSequence Analysis DNABlotting Northernbiology.organism_classificationAcetolactate decarboxylaseAcetolactate SynthaseRNA BacterialOpen reading framePhenotypeBiochemistryGenes BacterialLactatesLeuconostocFEMS Microbiology Letters
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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
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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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Spatial and temporal changes in Actinobacterial dominance in experimental artificial groundwater recharge.

2008

Abstract Artificial groundwater recharge (AGR) is used in the drinking water industry to supplement groundwater resources and to minimise the use of chemicals in water treatment. This study analysed the spatial and temporal changes of microbial communities in AGR using two test systems: a nutrient-amended fluidized-bed reactor (FBR) and a sand column. Structural changes in the feed lake water (Lake Roine), FBR, and sand column bacterial communities were determined by denaturing gradient gel electrophoresis (DGGE) and the length heterogeneity analysis of amplified 16S rRNA genes (LH-PCR). Two clone libraries were created to link the LH-PCR results to the dominant bacterial groups. The lake w…

DNA BacterialConservation of Natural ResourcesEnvironmental EngineeringFresh WaterBiologyPolymerase Chain ReactionWater SupplyRNA Ribosomal 16SDominance (ecology)Cloning MolecularWaste Management and DisposalFinlandPhylogenyWater Science and TechnologyCivil and Structural EngineeringDNA PrimersEcologyEcological ModelingCommunity structureGroundwater rechargePollutionActinobacteriaRNA BacterialMicrobial population biologyGenes BacterialbacteriaWater treatmentWater MicrobiologySurface waterGroundwaterTemperature gradient gel electrophoresisWater research
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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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Rapid molecular dissection of viral and bacterial immunomes

2006

The development of preventive or therapeutic recombinant vaccines and the generation of serodiagnostic assays for infectious diseases depend essentially on the availability of molecularly defined antigens. A major bottleneck for the identification of suitable target antigens for many pathogens is the isolation of sufficient amounts of material for subsequent genomic or proteomic screening. Applying a highly efficient expression cloning strategy to the human pathogens vaccinia virus (VV) and Chlamydia pneumoniae (CP), we demonstrate that sub-nanogram amounts of isolated nucleic acids can be utilized to determine comprehensive sets of immunodominant antigens. Remarkably, the approach not only…

DNA BacterialMaleBlotting WesternMolecular Sequence DataImmunologyEpitopes T-LymphocyteVaccinia virusBiologymedicine.disease_causePolymerase Chain ReactionViruslaw.inventionMicechemistry.chemical_compoundAntigenlawmedicineAnimalsHumansImmunology and AllergyCloning MolecularAntigens ViralPolymerase chain reactionAntigens BacterialBase SequenceImmunodominant EpitopesImmunogenicityChlamydophila pneumoniaeVirologyCTL*chemistryChlamydophila pneumoniaeDNA ViralExpression cloningFemaleVacciniaEuropean Journal of Immunology
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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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