Search results for "Bacterial Protein"

showing 10 items of 616 documents

Diversity and technological potential of lactic acid bacteria of wheat flours

2013

Abstract Lactic acid bacteria (LAB) were analysed from wheat flours used in traditional bread making throughout Sicily (southern Italy). Plate counts, carried out in three different media commonly used to detect food and sourdough LAB, revealed a maximal LAB concentration of approximately 4.75 Log CFU g−1. Colonies representing various morphological appearances were isolated and differentiated based on phenotypic characteristics and genetic analysis by randomly amplified polymorphic DNA (RAPD)-PCR. Fifty unique strains were identified. Analysis by 16S rRNA gene sequencing grouped the strains into 11 LAB species, which belonged to six genera: Enterococcus, Lactobacillus, Lactococcus, Leucono…

WeissellaLactococcusFlourLeuconostoc pseudomesenteroidesmedicine.disease_causeMicrobiologyMicrobiologyAcidificationWheat flourIndustrial MicrobiologyBacterial ProteinsLeuconostoc citreumLactobacillusmedicineLactic acid bacteriaLeuconostocLactic AcidWeissella cibariaProteolysiAcidification; Lactic acid bacteria; Proteolysis; Sourdough; Volatile organic compounds; Wheat flourPhylogenyTriticumbiologyfood and beveragesBiodiversitySettore AGR/15 - Scienze E Tecnologie AlimentariVolatile organic compoundbiology.organism_classificationLactobacillaceaeSourdoughPediococcusAcidsPeptide HydrolasesFood ScienceSettore AGR/16 - Microbiologia Agraria
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NovelAmycolatopsis balhimycinabiochemical abilities unveiled by proteomics

2014

Amycolatopsis balhimycina DSM5908 is an actinomycete producer of balhimycin, an analogue of vancomycin, the antibiotic of ‘last resort’ against multidrug-resistant Gram-positive pathogens. Most knowledge on glycopeptide biosynthetic pathways comes from studies on A. balhimycina as this strain, among glycopeptide producers, is genetically more amenable. The recent availability of its genome sequence allowed to perform differential proteomic analyses elucidating key metabolic pathways leading to antibiotic production in different growth conditions. To implement proteomic data on A. balhimycina derived from 2-DE approaches and to identify novel components, a combined approach based on protein …

Whole genome sequencingchemistry.chemical_classificationSpectrometry Mass Electrospray Ionizationmass spectrometry; 1D-electrophoresis; glycopeptide antibiotics; actinomycetes; glutamate dehydrogenaseProteomeBiologyProteomicsMicrobiologyGenomeActinomycetes proteomics 2D-DIGE Mass spectrometryGlycopeptideSynthetic biologyMetabolic pathwayEnzymeBiochemistrychemistryBacterial ProteinsTandem Mass SpectrometryProtein purificationActinomycetalesGeneticsElectrophoresis Polyacrylamide GelMolecular BiologyMetabolic Networks and Pathways
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Cutting Edge: An IL-17F-CreEYFP Reporter Mouse Allows Fate Mapping of Th17 Cells

2009

Abstract The need for reporter lines able to faithfully track Th17 cells in vivo has become an issue of exceptional importance. To address this, we generated a mouse strain in which Cre recombinase is expressed from the IL-17F promoter. Crossing the IL-17F-Cre allele to a conditional enhanced yellow fluorescent protein (EYFP) reporter mouse yielded the IL-17F-CreEYFP strain, in which IL-17F expression is twinned with EYFP in live IL-17F-expressing cells. Although we demonstrate that IL-17F expression is restricted to CD4+ T cells during experimental autoimmune encephalomyelitis, IL-17F-CreEYFP CD8 T cells robustly expressed IL-17F in response to TGF-β, IL-6, and IL-23. Fate mapping of IL-17…

Yellow fluorescent proteinAdoptive cell transferEncephalomyelitis Autoimmune ExperimentalRNA UntranslatedTransgeneImmunologyCre recombinaseMice TransgenicCD8-Positive T-LymphocytesT-Lymphocytes RegulatoryImmunophenotypingMiceBacterial ProteinsGenes ReporterFate mappingAnimalsHumansImmunology and AllergyCytotoxic T cellCells CulturedIntegrasesbiologyInterleukin-17ProteinsCell DifferentiationAdoptive TransferMolecular biologyPhenotypeIn vitroMice Inbred C57BLLuminescent ProteinsGene Expression RegulationMice Inbred DBAbiology.proteinThe Journal of Immunology
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Polar accumulation of the metabolic sensory histidine kinases DcuS and CitA in Escherichia coli

2008

Signal transduction in prokaryotes is frequently accomplished by two-component regulatory systems in which a histidine protein kinase is the sensory component. Many of these sensory kinases control metabolic processes that do not show an obvious requirement for inhomogeneous distribution within bacterial cells. Here, the sensory kinases DcuS and CitA, two histidine kinases of Escherichia coli, were investigated. Both are membrane-integral and involved in the regulation of carboxylate metabolism. The two-component sensors were fused with yellow fluorescent protein (YFP) and live images of immobilized cells were obtained by confocal laser fluorescence microscopy. The fluorescence of the fusio…

Yellow fluorescent proteinbiologyKinaseEscherichia coli ProteinsRecombinant Fusion ProteinsCell PolarityMicrobiologyFusion proteinLuminescent ProteinsProtein TransportBacterial ProteinsBiochemistryCytoplasmEscherichia colibiology.proteinSignal transductionCell fractionationProtein kinase AProtein KinasesHistidineMicrobiology
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Efficient, non-toxic anion transport by synthetic carriers in cells and epithelia.

2016

Transmembrane anion transporters (anionophores) have potential for new modes of biological activity, including therapeutic applications. In particular they might replace the activity of defective anion channels in conditions such as cystic fibrosis. However, data on the biological effects of anionophores are scarce, and it remains uncertain whether such molecules are fundamentally toxic. Here, we report a biological study of an extensive series of powerful anion carriers. Fifteen anionophores were assayed in single cells by monitoring anion transport in real time through fluorescence emission from halide-sensitive yellow fluorescent protein. A bis-(p-nitrophenyl)ureidodecalin shows especial…

Yellow fluorescent proteinpotencyGeneral Chemical Engineeringsynthetic anion carriersCystic Fibrosis Transmembrane Conductance Regulator01 natural sciencesMadin Darby Canine Kidney CellsCell membranedeliverabilityta116Drug CarriersbiologyMolecular StructureChemistryBiological activitypersistenceCystic fibrosis transmembrane conductance regulatorTransmembrane proteinanionophoresmedicine.anatomical_structureBiochemistryPhosphatidylcholinesSteroidsChlorineAnionsCell SurvivalNaphthalenesta3111010402 general chemistryDogsBacterial ProteinsCyclohexanesmedicineAnimalsHumansIon transporterCell ProliferationIon Transport010405 organic chemistryCell MembranetoxicityTransporterEpithelial CellsHydrogen BondingGeneral ChemistryRats Inbred F3440104 chemical sciencesElectrophysiological PhenomenaLuminescent ProteinsMicroscopy FluorescenceCell cultureDrug Designbiology.proteinHeLa CellsNature chemistry
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Acyl-homoserine lactone production is more common among plant-associated Pseudomonas spp. than among soilborne Pseudomonas spp.

2001

ABSTRACT A total of 137 soilborne and plant-associated bacterial strains belonging to different Pseudomonas species were tested for their ability to synthesize N -acyl-homoserine lactones (NAHL). Fifty-four strains synthesized NAHL. Interestingly, NAHL production appears to be more common among plant-associated than among soilborne Pseudomonas spp. Indeed, 40% of the analyzed Pseudomonas syringae strains produced NAHL which were identified most often as the short-chain NAHL, N -hexanoyl- l -homoserine lactone, N -(3-oxo-hexanoyl)-homoserine lactone, and N -(3-oxo-octanoyl)- l -homoserine lactone (no absolute correlation between genomospecies of P. syringae and their ability to produce NAHL …

[ SDV.BV ] Life Sciences [q-bio]/Vegetal BiologyMESH: Sequence Analysis DNAMESH : Molecular Sequence DataMESH: PlantsMESH: Amino Acid SequenceErwiniaMESH: Base SequenceApplied Microbiology and Biotechnologychemistry.chemical_compoundPlant MicrobiologyMESH: Plant Diseases4-ButyrolactoneChromobacteriumPseudomonas syringaeMESH : Bacterial ProteinsMESH : DNA BacterialCloning MolecularMESH: Bacterial ProteinsComputingMilieux_MISCELLANEOUSSoil Microbiology[SDV.EE]Life Sciences [q-bio]/Ecology environment0303 health sciencesMESH: Gene Expression Regulation BacterialMESH: Genetic Complementation TestEcologybiologyMESH : Amino Acid SequenceMESH : Plant DiseasesPseudomonasBacterialMESH : 4-ButyrolactonePlantsN-ACYL-HOMOSERINE LACTONE[SDV.EE] Life Sciences [q-bio]/Ecology environmentPseudomonadalesSequence AnalysisBiotechnologyPseudomonadaceaeMESH : Gene Expression Regulation BacterialDNA BacterialMESH : Cloning MolecularMESH : Soil MicrobiologyCarbon-Oxygen LyasesMolecular Sequence DataHomoserineMESH : PlantsMicrobiologyMESH: Carbon-Oxygen Lyases03 medical and health sciencesBacterial ProteinsPseudomonas[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyMESH: Cloning MolecularAmino Acid SequenceMESH : Carbon-Oxygen Lyases030304 developmental biologyPlant DiseasesMESH: Molecular Sequence DataMESH : Genetic Complementation TestBase Sequence030306 microbiologyPantoeaGenetic Complementation TestMolecularMESH: PseudomonasGene Expression Regulation BacterialSequence Analysis DNADNAbiology.organism_classificationMESH: DNA BacterialchemistryGene Expression RegulationMESH: Soil MicrobiologyMESH: 4-ButyrolactoneMESH : Base SequenceFood ScienceMESH : PseudomonasMESH : Sequence Analysis DNACloning
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Relationships between Staphylococcus aureus genetic background, virulence factors, agr groups (alleles), and human disease

2002

ABSTRACT The expression of most Staphylococcus aureus virulence factors is controlled by the agr locus, which encodes a two-component signaling pathway whose activating ligand is an agr -encoded autoinducing peptide (AIP). A polymorphism in the amino acid sequence of the AIP and of its corresponding receptor divides S. aureus strains into four major groups. Within a given group, each strain produces a peptide that can activate the agr response in the other member strains, whereas the AIPs belonging to different groups are usually mutually inhibitory. We investigated a possible relationship between agr groups and human S. aureus disease by studying 198 S. aureus strains isolated from 14 asym…

[SDE] Environmental SciencesStaphylococcus aureus[SDV.OT]Life Sciences [q-bio]/Other [q-bio.OT][SDV]Life Sciences [q-bio]Bacterial ToxinsImmunologyVirulenceLocus (genetics)Biologymedicine.disease_causeMicrobiologylaw.inventionMicrobiology03 medical and health sciencesBacterial ProteinslawPhylogeneticsmedicineHumansAllelePeptide sequenceComputingMilieux_MISCELLANEOUSAllelesPhylogenyPolymerase chain reaction030304 developmental biologyGenetics0303 health sciencesVirulence030306 microbiologyBacterial InfectionsStaphylococcal Infectionsbiochemical phenomena metabolism and nutritionbacterial infections and mycoses[SDV] Life Sciences [q-bio]Infectious DiseasesPOUVOIR PATHOGENEStaphylococcus aureus[SDE]Environmental SciencesTrans-ActivatorsbacteriaFemaleParasitologyAmplified fragment length polymorphismSignal Transduction
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Inactivation of PadR, the repressor of the phenolic acid stress response, by molecular interaction with Usp1, a universal stress protein from Lactoba…

2009

ABSTRACT The phenolic acid decarboxylase gene padA is involved in the phenolic acid stress response (PASR) in gram-positive bacteria. In Lactobacillus plantarum , the padR gene encodes the negative transcriptional regulator of padA and is cotranscribed with a downstream gene, usp1 , which encodes a putative universal stress protein (USP), Usp1, of unknown function. The usp1 gene is overexpressed during the PASR. However, the role and the mechanism of action of the USPs are unknown in gram-positive bacteria. Therefore, to gain insights into the role of USPs in the PASR; (i) a usp1 deletion mutant was constructed; (ii) the two genes padR and usp1 were coexpressed with padA under its own promo…

[SDV.BIO]Life Sciences [q-bio]/BiotechnologyCarboxy-LyasesMolecular Sequence DataRepressorGenetics and Molecular Biologymedicine.disease_causeApplied Microbiology and Biotechnology03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsHydroxybenzoatesTranscriptional regulationmedicineEscherichia coliAmino Acid SequenceGene SilencingGeneEscherichia coliHeat-Shock Proteins030304 developmental biologyRegulation of gene expression0303 health sciencesReporter geneEcologybiology030306 microbiologyGene Expression Regulation BacterialPhenolic acidbiology.organism_classificationMolecular biologyEnterobacteriaceaeacide phénolique[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologychemistryBiochemistryMutationSequence AlignmentHeat-Shock ResponseLactobacillus plantarumFood ScienceBiotechnologyexpression des gènes
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Biochemical and structural features of a novel cyclodextrinase from cow rumen metagenome.

2007

A novel enzyme, RA.04, belonging to the alpha-amylase family was obtained after expression of metagenomic DNA from rumen fluid (Ferrer et al.: Environ. Microbiol. 2005, 7, 1996-2010). The purified RA.04 has a tetrameric structure (280 kDa) and exhibited maximum activity (5000 U/mg protein) at 70 degrees C and was active within an unusually broad pH range from 5.5 to 9.0. It maintained 80% activity at pH 5.0 and 9.5 and 75 degrees C. The enzyme hydrolyzed alpha-D-(1,4) bonds 13-fold faster than alpha-D-(1,6) bonds to yield maltose and glucose as the main products, and it exhibited transglycosylation activity. Its preferred substrates, in the descending order, were maltooligosaccharides (C3-C…

alpha-CyclodextrinsRumenGlycoside HydrolasesStarchAmylopectinOligosaccharidesApplied Microbiology and BiotechnologyCatalysisSubstrate Specificitychemistry.chemical_compoundBacterial ProteinsAmyloseCyclomaltodextrinaseAnimalsMaltoseGlucansChromatography High Pressure Liquidchemistry.chemical_classificationBinding Sitesbiologybeta-CyclodextrinsTemperatureActive sitePullulanStarchGeneral MedicineMaltoseHydrogen-Ion ConcentrationEnzymechemistryBiochemistryAmylopectinbiology.proteinMolecular MedicineCattleElectrophoresis Polyacrylamide GelAmylosegamma-CyclodextrinsBiotechnology journal
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The L-tartrate/succinate antiporter TtdT (YgjE) of L-tartrate fermentation in Escherichia coli.

2007

ABSTRACT Escherichia coli ferments l -tartrate under anaerobic conditions in the presence of an additional electron donor to succinate. The carrier for l -tartrate uptake and succinate export and its relation to the general C 4 -dicarboxylate carriers DcuA, DcuB, and DcuC were studied. The secondary carrier TtdT, encoded by the ttdT (previously called ygjE ) gene, is required for the uptake of l -tartrate. The ttdT gene is located downstream of the ttdA and ttdB genes, encoding the l -tartrate dehydratase TtdAB. Analysis of mRNA by reverse transcription-PCR showed that ttdA , ttdB , and ttdT are cotranscribed. Deletion of ttdT abolished growth by l -tartrate and degradation of l -tartrate c…

biologyAntiporterPhysiology and MetabolismSuccinic AcidHeterologousSubstrate (chemistry)Biological TransportTartratebiology.organism_classificationmedicine.disease_causeMicrobiologychemistry.chemical_compoundBiochemistrychemistryBacterial ProteinsDehydrataseFermentationOperonmedicineEscherichia coliFermentationMolecular BiologyEscherichia coliTartratesBacteriaJournal of bacteriology
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