Search results for "Bacillus"

showing 10 items of 774 documents

The proteome and transcriptome analysis ofBacillus subtilis in response to salicylic acid

2007

Phenolic acids that are present in plant-soil ecosystems can be considered as toxins which induce specific stress responses in microorganisms. In this paper, we have analyzed the global response of the soil bacterium Bacillus subtilis to salicylic acid using proteomics and transcriptomics. The results demonstrate that salicylic acid caused predominantly the induction of the SigmaB-dependent general stress response in B. subtilis which is not related to the acidic conditions. Treatment of B. subtilis with growth-inhibitory concentrations of 4 mM salicylic acid caused protein damage in B. subtilis as reflected by the induction of the CtsR and Spx regulons. Both phenolic acid decarboxylases (p…

Carboxy-lyasesBacillaceaeProteomebiologyOperonBacillus subtilisPhenolic acidHydrogen-Ion Concentrationbiology.organism_classificationBiochemistrychemistry.chemical_compoundRegulonAnti-Infective AgentschemistryBiochemistryRNASalicylic AcidMolecular BiologyBacteriaSalicylic acidBacillus subtilisPROTEOMICS
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Phenolic Acid-Mediated Regulation of the padC Gene, Encoding the Phenolic Acid Decarboxylase of Bacillus subtilis

2008

ABSTRACT In Bacillus subtilis , several phenolic acids specifically induce expression of padC , encoding a phenolic acid decarboxylase that converts these antimicrobial compounds into vinyl derivatives. padC forms an operon with a putative coding sequence of unknown function, yveFG , and this coding sequence does not appear to be involved in the phenolic acid stress response (PASR). To identify putative regulators involved in the PASR, random transposon mutagenesis, combined with two different screens, was performed. PadR, a negative transcriptional regulator of padC expression, was identified. padR is not located in the vicinity of padC , and the expression of padR is low and appears const…

Carboxy-lyasesCarboxy-LyasesOperonMolecular Sequence DataElectrophoretic Mobility Shift AssayBacillus subtilisBiologyMicrobiologyGene Expression Regulation Enzymologic03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsHydroxybenzoatesGene RegulationElectrophoretic mobility shift assay[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceMolecular Biology030304 developmental biologychemistry.chemical_classification0303 health sciencesBase Sequence030306 microbiologyEffectorGene Expression Regulation BacterialPhenolic acidbiology.organism_classificationMolecular biologyRepressor ProteinsEnzymechemistryBiochemistryTransposon mutagenesisBacillus subtilis
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Expression in Escherichia coli of Native and Chimeric Phenolic Acid Decarboxylases with Modified Enzymatic Activities and Method for Screening Recomb…

2001

ABSTRACT Four bacterial phenolic acid decarboxylases (PAD) from Lactobacillus plantarum , Pediococcus pentosaceus , Bacillus subtilis , and Bacillus pumilus were expressed in Escherichia coli , and their activities on p -coumaric, ferulic, and caffeic acids were compared. Although these four enzymes displayed 61% amino acid sequence identity, they exhibit different activities for ferulic and caffeic acid metabolism. To elucidate the domain(s) that determines these differences, chimeric PAD proteins were constructed and expressed in E. coli by exchanging their individual carboxy-terminal portions. Analysis of the chimeric enzyme activities suggests that the C-terminal region may be involved …

Carboxy-lyasesCoumaric AcidsCarboxy-LyasesDecarboxylationRecombinant Fusion ProteinsBacillus subtilismedicine.disease_causeApplied Microbiology and BiotechnologySubstrate Specificitychemistry.chemical_compoundCaffeic AcidsEscherichia coliCaffeic acidmedicineAmino Acid SequenceEnzymology and Protein EngineeringEscherichia colichemistry.chemical_classificationBacteriaEcologybiologyBacillus pumilusSequence Analysis DNAPhenolic acidbiology.organism_classificationCulture MediaEnzymechemistryBiochemistryFood ScienceBiotechnologyApplied and Environmental Microbiology
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Knockout of thep-Coumarate Decarboxylase Gene fromLactobacillus plantarumReveals the Existence of Two Other Inducible Enzymatic Activities Involved i…

2000

ABSTRACTLactobacillus plantarumNC8 contains apdcgene coding forp-coumaric acid decarboxylase activity (PDC). A food grade mutant, designated LPD1, in which the chromosomalpdcgene was replaced with the deletedpdcgene copy, was obtained by a two-step homologous recombination process using an unstable replicative vector. The LPD1 mutant strain remained able to weakly metabolizep-coumaric and ferulic acids into vinyl derivatives or into substituted phenyl propionic acids. We have shown thatL. plantarumhas a second acid phenol decarboxylase enzyme, better induced with ferulic acid than withp-coumaric acid, which also displays inducible acid phenol reductase activity that is mostly active when gl…

Carboxy-lyasesCoumaric AcidsCarboxy-LyasesMutantGenetics and Molecular Biologymacromolecular substancesCoumaric acidApplied Microbiology and BiotechnologyFerulic acidchemistry.chemical_compoundHydroxybenzoatesCloning Molecularchemistry.chemical_classificationEcologybiologyhemic and immune systemsMetabolismPhenolic acidHydrogen-Ion Concentrationbiology.organism_classificationLactobacillusElectroporationEnzymechemistryBiochemistryEnzyme InductionPropionatesOxidoreductasesGene DeletionLactobacillus plantarumFood ScienceBiotechnologyApplied and Environmental Microbiology
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Kinetics and Intensity of the Expression of Genes Involved in the Stress Response Tightly Induced by Phenolic Acids in <i>Lactobacillus plantar…

2007

In <i>Lactobacillus plantarum</i>, PadR, the negative transcriptional regulator of <i>padA </i>encoding the phenolic acid decarboxylase, is divergently oriented from <i>padA. </i>Moreover, it forms an operonic structure with <i>usp1,</i> a genewhose products display homology with proteins belonging to the UspA family of universal stress proteins. PadR is inactivated by the addition of <i>p-</i>coumaric, ferulic or caffeic acid to the culture medium. In order to better characterize the stress response of this bacterium to phenolic acids, we report here the kinetics and quantitative expression by qRT-PCR of the 3 genes from the <i…

Carboxy-lyasesPhysiologymedicine.disease_causeApplied Microbiology and BiotechnologyBiochemistryMicrobiology03 medical and health scienceschemistry.chemical_compoundHeat shock proteinGene expressionmedicineCaffeic acidEscherichia coliGene030304 developmental biology0303 health sciencesbiology030306 microbiologyCell BiologyPhenolic acidbiology.organism_classificationMolecular biologychemistryBiochemistryLactobacillus plantarumBiotechnologyMicrobial Physiology
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Improved model based on the Weibull distribution to describe the combined effect of pH and temperature on the heat resistance of Bacillus cereus in c…

2003

The effect of pH and temperature on the thermal inactivation of different strains of Bacillus cereus was modeled. Inactivation tests were carried out in carrot broth, following a full factorial design at four levels for temperature (from 90 to 105 degrees C, depending on the strain) and pH (6.2, 5.8, 5.2, and 4.7). Individual inactivation curves were analyzed by applying the Weibull model function (with percent discrepancy close to 20% for most cases), and the effects of pH and temperature on the scale parameter (designated D(beta)) and the shape parameter (beta) were also studied. Temperature and pH did not have a significant effect on the shape parameter (beta). The effect of temperature …

Carrot juiceHot TemperatureBacillus cereusThermodynamicsModels BiologicalMicrobiologyShape parameterBeveragesBacillus cereusWeibull distributionStrain (chemistry)biologybusiness.industryChemistryFactorial experimentHydrogen-Ion Concentrationbiology.organism_classificationDaucus carotaBiotechnologyKineticsCereusFood MicrobiologybusinessScale parameterStatistical DistributionsFood Science
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Bacillus thuringiensis Cry1Ac Toxin-Binding and Pore-Forming Activity in Brush Border Membrane Vesicles Prepared from Anterior and Posterior Midgut R…

2008

ABSTRACT It is generally accepted that Bacillus thuringiensis Cry toxins insert into the apical membrane of the larval midgut after binding to specific receptors, and there is evidence that the distribution of binding molecules along the midgut is not uniform. By use of the voltage-sensitive dye DiSC 3 (5) and 125 I-labeled Cry1Ac, we have measured the effect of Cry1Ac in terms of permeabilization capacity and of binding parameters on brush border membrane vesicles (BBMV) prepared from the anterior and the posterior regions of the larval midgut from two insect species, Manduca sexta and Helicoverpa armigera . The permeabilizing activity was significantly higher with BBMV from the posterior …

Cell Membrane PermeabilityBrush bordermedia_common.quotation_subjectBacterial ProteinInsectApplied Microbiology and BiotechnologyIodine RadioisotopeIodine RadioisotopesHemolysin ProteinsEndotoxinBacterial ProteinsManducaBacillus thuringiensisInvertebrate MicrobiologyAnimalsmedia_commonBacillus thuringiensis ToxinsMicrovilliEcologybiologyAnimalVesiclefungiMidgutHemolysin ProteinApical membraneAlkaline Phosphatasebiology.organism_classificationEndotoxinsEnzyme ActivationLepidopteraBiochemistryManduca sextaLarvaPotassiumBiophysicsManducaDigestive SystemProtein BindingFood ScienceBiotechnologyApplied and Environmental Microbiology
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Toxicity and mode of action of Bacillus thuringiensis Cry proteins in the Mediterranean corn borer, Sesamia nonagrioides (Lefebvre)

2006

ABSTRACT Sesamia nonagrioides is one of the most damaging pests of corn in Spain and other Mediterranean countries. Bt corn expressing the Bacillus thuringiensis Cry1Ab toxin is being grown on about 58,000 ha in Spain. Here we studied the mode of action of this Cry protein on S. nonagrioides (binding to specific receptors, stability of binding, and pore formation) and the modes of action of other Cry proteins that were found to be active in this work (Cry1Ac, Cry1Ca, and Cry1Fa). Binding assays were performed with 125 I- or biotin-labeled toxins and larval brush border membrane vesicles (BBMV). Competition experiments indicated that these toxins bind specifically and that Cry1Aa, Cry1Ab, an…

Cell Membrane PermeabilityMembrane permeabilityBacterial ToxinsBacillus thuringiensisSesamia nonagrioidesBacterial ToxinBacterial ProteinZea maysApplied Microbiology and BiotechnologyOstriniaHemolysin ProteinsZea mayBacterial ProteinsEndotoxinBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsBacillus thuringiensiBinding siteMode of actionPest Control BiologicalGenetically modified maizeBacillus thuringiensis ToxinsEcologybiologyMicrovilliAnimalfungifood and beveragesHemolysin Proteinbiology.organism_classificationPlants Genetically ModifiedEndotoxinsLepidopteraCry1AcBiochemistryLarvaFood ScienceBiotechnology
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CtsR is the master regulator of stress response gene expression in Oenococcus oeni.

2005

ABSTRACT Although many stress response genes have been characterized in Oenococcus oeni , little is known about the regulation of stress response in this malolactic bacterium. The expression of eubacterial stress genes is controlled both positively and negatively at the transcriptional level. Overall, negative regulation of heat shock genes appears to be more widespread among gram-positive bacteria. We recently identified an ortholog of the ctsR gene in O. oeni . In Bacillus subtilis , CtsR negatively regulates expression of the clp genes, which belong to the class III family of heat shock genes. The ctsR gene of O. oeni is cotranscribed with the downstream clpC gene. Sequence analysis of t…

ChaperoninsOperonMolecular Sequence DataBiologyMicrobiologyGenome03 medical and health sciencesBacterial ProteinsSigma factorHeat shock proteinOperon[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyGene RegulationPromoter Regions GeneticMolecular BiologyGeneHeat-Shock Proteins030304 developmental biologyRegulator geneOenococcus oeniGeneticsRegulation of gene expressionAdenosine Triphosphatases0303 health sciencesBase Sequence030306 microbiologyCTSRGene Expression Regulation Bacterialbiology.organism_classificationDNA-Binding ProteinsGram-Positive CocciRepressor ProteinsMutagenesis Site-DirectedOenococcus oeniGenome BacterialHeat-Shock ResponseBacillus subtilisMolecular ChaperonesJournal of bacteriology
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Effect of the natural winemaking process applied at industrial level on the microbiological and chemical characteristics of wine.

2013

The composition of yeast and lactic acid bacteria (LAB) communities and the chemical evolution of the large-scale commercial vinification of Catarratto IGT Sicilia, carried out under the biological regime, was followed from grape harvest until bottling. Simultaneously to the maximum growth of yeasts, LAB counts reached high level of concentration (6-7 log CFU mL(-1)) during the first steps of the alcoholic fermentation. Yeast identification was determined applying different molecular methods. The highest species biodiversity was observed on grape and must samples taken soon after pressing. Saccharomyces cerevisiae was detected at dominant concentrations during the entire winemaking process.…

Chemical analysiColony Countved/biology.organism_classification_rank.speciesColony Count MicrobialCatarratto grapevine; Chemical analysis; Lactic acid bacteria; Lactobacillus plantarum; Natural wine; Saccharomyces cerevisiae; Sicily; Spontaneous fermentation; Yeasts; Biodiversity; Colony Count Microbial; Ethanol; Fermentation; Italy; Lactobacillaceae; Leuconostoc; Phenols; Vitis; Volatile Organic Compounds; Wine; Yeasts; Food-Processing IndustryBioengineeringWineLactic acid bacteria; Yeasts; Lactobacillus plantarum; Saccharomyces cerevisiae; Chemical analysis; Spontaneous fermentation; Catarratto grapevine; Sicily; Natural wineLactobacillus hilgardiiSaccharomyces cerevisiaeEthanol fermentationSpontaneous fermentationApplied Microbiology and BiotechnologyMicrobialPhenolsYeastsMaceration (wine)Lactic acid bacteriaLeuconostocChemical analysisVitisFood scienceFood-Processing IndustrySicilyWinemakingCatarratto grapevineVolatile Organic CompoundsbiologyEthanolved/biologyfood and beveragesSettore AGR/15 - Scienze E Tecnologie AlimentariBiodiversitybiology.organism_classificationYeastBiochemistryItalyLeuconostoc mesenteroidesLactobacillaceaeFermentationNatural wineFermentationLactobacillus plantarumLeuconostocBiotechnologyLactobacillus plantarumSettore AGR/16 - Microbiologia AgrariaJournal of bioscience and bioengineering
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