Search results for "subtil"

showing 10 items of 108 documents

Antibacterial activity of the emerging Fusarium mycotoxins enniatins A, A1, A2, B, B1, and B4 on probiotic microorganisms

2014

Abstract Enniatins (ENs) are secondary metabolites produced by several Fusarium strains, chemically characterized as N-methylated cyclohexadepsipeptides. These compounds are known to act as antifungal and antibacterial agents, but they also possess anti-insect and phytotoxic properties. In this study, the antimicrobial effect of pure fractions of the bioactive compounds ENs A, A 1 , A 2 , B, B 1 , and B 4 was tested towards nine probiotic microrganisms, twenty-two Saccharomyces cerevisiae strains and nine Bacillus subtilis strains. Antimicrobial analyses were carried out the disc-diffusion method using ENs concentrations ranging from 0.2 to 20,000 ng. Plates were incubated for 24 h at 37 °C…

FusariumbiologyMicroorganismBacillus subtilisBacterial growthToxicologybiology.organism_classificationAntimicrobialMicrobiologylaw.inventionchemistry.chemical_compoundProbioticchemistrylawMycotoxinAntibacterial activityToxicon
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Phosphororganische Verbindungen, 110. Gezielte Fluoreszenzmarkierung von Serin-Enzymen

1985

Verbindungen vom Typ R1R2P(O)X [X = F, OC6H4NO2-(4)] sind OH-selektiv und reagieren mit der Serinhydroxygruppe im aktiven Zentrum von Esterasen (α-Chymotrypsin, Trypsin, Butyrylcholinesterase, Acetylcholinesterase und Subtilisin) unter Bildung des entsprechenden inaktiven Phosphorylesters [R1R2P(O)-O-Ser-Esterase]. Mit R1 = 5-(Dimethylamino)naphthyl bzw. 5-Methoxynaphthyl und R2 = Alkyl, Aryl, O-Alkyl erhalt man die chemoselektiven, fluoreszierenden Reagenzien 1–7, welche die oben genannten Esterasen spezifisch hemmen. Es wurde a) die Abhangigkeit der Inhibierung von der Konzentration der Inhibitoren bestimmt und b) durch Gelelektrophorese des inhibierten Enzyms gezeigt, das der fluoreszier…

Gel electrophoresischemistry.chemical_classificationbiologyStereochemistryArylOrganic ChemistrySubtilisinActive siteTrypsinEsteraseSerinechemistry.chemical_compoundEnzymechemistrybiology.proteinmedicinePhysical and Theoretical Chemistrymedicine.drugLiebigs Annalen der Chemie
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Demonstration that the Group II Intron from the Clostridial Conjugative Transposon Tn5397 Undergoes Splicing In Vivo

2001

Previous work has identified the conjugative transposon Tn5397 from Clostridium difficile. This element was shown to contain a group II intron. Tn5397 can be conjugatively transferred from C. difficile to Bacillus subtilis. In this work we show that the intron is spliced in both these hosts and that nonspliced RNA is also present. We constructed a mutation in the open reading frame within the intron, and this prevented splicing but did not prevent the formation of the circular form of the conjugative transposon (the likely transposition intermediate) or decrease the frequency of intergeneric transfer of Tn5397. Therefore, the intron is spliced, but splicing is not required for conjugation o…

GeneticsTransposable elementMutationClostridioides difficileRNA SplicingIntronRNAGroup II intronBiologymedicine.disease_causeMicrobiologyIntronsTransposition (music)Open reading frameRNA BacterialConjugation GeneticRNA splicingmedicineDNA Transposable ElementsRNA MessengerMolecular BiologyPlasmids and TransposonsBacillus subtilis
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Identification of Two Mannoproteins Released from Cell Walls of a Saccharomyces cerevisiae mnn1 mnn9 Double Mutant by Reducing Agents

1999

The cell wall of Saccharomyces cerevisiae represents some 30% of the total weight of the cell and is made up of β-glucans, mannose-containing glycoproteins (mannoproteins), and small amounts of chitin (9, 15). The mannoproteins can be divided into three groups according to the linkages that bind them to the structure of the cell wall: (i) noncovalently bound, (ii) covalently bound to the structural glucan, and (iii) disulfide bound to other proteins that are themselves covalently bound to the structural glucan of the cell wall (8). Our work has focused on the disulfide-bound mannoproteins, probably the least well known of the three groups mentioned above. Previous work (25) showed that trea…

GlycosylationSaccharomyces cerevisiae ProteinsGlycosylationBlotting WesternMolecular Sequence DataSaccharomyces cerevisiaeSaccharomyces cerevisiaeMicrobiologyGene Expression Regulation EnzymologicFungal ProteinsCell wallOpen Reading FramesSurface-Active Agentschemistry.chemical_compoundCell WallGene Expression Regulation FungalEndopeptidasesAspartic Acid EndopeptidasesAmino Acid SequenceSubtilisinsFluorescent Antibody Technique IndirectMolecular BiologyMercaptoethanolGlucanGel electrophoresischemistry.chemical_classificationFungal proteinMembrane GlycoproteinsbiologySodium Dodecyl SulfateBiological Transportbiology.organism_classificationRecombinant ProteinsYeastMolecular Weightcarbohydrates (lipids)Cytoskeletal ProteinsEukaryotic CellsPhenotypechemistryBiochemistryMutagenesisReducing AgentsElectrophoresis Polyacrylamide GelProprotein ConvertasesProtein Tyrosine PhosphatasesGlycoproteinGene DeletionJournal of Bacteriology
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Fumarate respiration of Wolinella succinogenes: enzymology, energetics and coupling mechanism.

2002

Wolinella succinogenes performs oxidative phosphorylation with fumarate instead of O2 as terminal electron acceptor and H2 or formate as electron donors. Fumarate reduction by these donors ('fumarate respiration') is catalyzed by an electron transport chain in the bacterial membrane, and is coupled to the generation of an electrochemical proton potential (Deltap) across the bacterial membrane. The experimental evidence concerning the electron transport and its coupling to Deltap generation is reviewed in this article. The electron transport chain consists of fumarate reductase, menaquinone (MK) and either hydrogenase or formate dehydrogenase. Measurements indicate that the Deltap is generat…

HydrogenaseStereochemistryBiophysicsOxidative phosphorylationCoupling mechanismFormate dehydrogenaseBiochemistryCatalysisOxidative PhosphorylationWolinella succinogenesElectron Transportchemistry.chemical_compoundFumaratesHydrogenaseFormatechemistry.chemical_classificationFumarate respirationBinding SitesbiologySuccinate dehydrogenaseCell MembraneVitamin K 2Cell BiologyElectron acceptorFumarate reductaseElectron transport chainFormate DehydrogenasesWolinellaSuccinate DehydrogenaseBiochemistrychemistryModels Chemicalbiology.proteinFormate dehydrogenaseEnergy MetabolismOxidation-ReductionBacillus subtilisBiochimica et biophysica acta
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Indicaciones de los inhibidores de PCSK9 en la práctica clínica. Recomendaciones de la Sociedad Española de Arteriosclerosis (SEA), 2019

2019

Resumen Un grupo de expertos convocado por la Sociedad Espanola de Arteriosclerosis (SEA) se ha encargado de actualizar el documento de la SEA sobre las indicaciones de los inhibidores de PCSK9 (iPCSK9) en la practica clinica publicadas en 2016. Esta actualizacion es necesaria porque en el periodo transcurrido hasta la actualidad se han publicado los resultados de los ensayos clinicos realizados a gran escala con iPCSK9 que demuestran que, ademas de su alta potencia para disminuir el colesterol aterogenico, disminuyen el riesgo de presentar episodios de enfermedad cardiovascular aterosclerotica en los pacientes con enfermedad tanto estable como reciente, y con un alto grado de seguridad. La…

Inhibidores de la proproteína convertasa subtilisina kexina 9ArteriosclerosisEnfermedad cardiovascularFamilial hypercholesterolemiaClinical indicationsLow density lipoprotein030204 cardiovascular system & hematologyArteriosclerosi03 medical and health sciencesLipoproteínas de baja densidad0302 clinical medicineIndicaciones clínicasTratamientoPharmacology (medical)030212 general & internal medicineConsensus documentHipercolesterolemia familiarNumber needed to treatCardiovascular diseaseDocumento de consensoTreatmentArterioesclerosiCholesterolProprotein convertase subtilisin kexin 9 inhibitorsCardiology and Cardiovascular MedicineColesterolNúmero necesario a tratar
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Genetic and Biochemical Analysis of PadR-padC Promoter Interactions during the Phenolic Acid Stress Response in Bacillus subtilis 168

2011

ABSTRACT Bacillus subtilis 168 is resistant to phenolic acids by expression of an inducible enzyme, the phenolic acid decarboxylase (PadC), that decarboxylates these acids into less toxic vinyl derivatives. In the phenolic acid stress response (PASR), the repressor of padC , PadR, is inactivated by these acids. Inactivation of PadR is followed by a strong expression of padC . To elucidate the functional interaction between PadR and the padC promoter, we performed (i) footprinting assays to identify the region protected by PadR, (ii) electrophoretic mobility shift assays (EMSAs) with a modified padC promoter protected region to determine the interacting sequences, and (iii) random mutagenesi…

Leucine zipperMutantRepressorElectrophoretic Mobility Shift AssayGenetics and Molecular BiologyBacillus subtilisBiologyMicrobiologyProtein Structure Secondary03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsStress PhysiologicalBacillus subtilis 168Hydroxybenzoates[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyPromoter Regions GeneticMolecular Biology030304 developmental biology2. Zero hungerchemistry.chemical_classification0303 health sciences030306 microbiologyMutagenesisPhenolic acidGene Expression Regulation Bacterialbiology.organism_classificationMolecular biologyFootprintingEnzymechemistryBiochemistryBacillus subtilisProtein Binding
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Gram-positive bacteria on grass pollen exhibit adjuvant activity inducing inflammatory T cell responses.

2011

BACKGROUND: Recently, it has been established that pollen grains contain Th2-enhancing activities besides allergens. OBJECTIVE: The aim of this study was to analyse whether pollen carry additional adjuvant factors like microbes and what immunological effects they may exert. METHODS: Timothy pollen grains were collected and disseminated on agar plates, and the growing microorganisms were cultivated and defined. Furthermore, the immunologic effects of microbial products on DC and T cell responses were analysed. RESULTS: A complex mixture of bacteria and moulds was detected on grass pollen. Besides Gram-negative bacteria that are known to favour Th1-directed immune responses, moulds were ident…

LipopolysaccharideT cellGram-positive bacteriaImmunologyBiologymedicine.disease_causeGram-Positive BacteriaLymphocyte ActivationMicrobiologychemistry.chemical_compoundImmune systemTh2 CellsAdjuvants ImmunologicBacillus cereusPollenotorhinolaryngologic diseasesmedicineImmunology and AllergyHumansInflammationfood and beveragesFOXP3Rhinitis Allergic SeasonalCell DifferentiationDendritic CellsTh1 Cellsbiology.organism_classificationFlow CytometryCulture Mediamedicine.anatomical_structurechemistryPhleumImmunologyPollenTh17 CellsCD80BacteriaBacillus subtilisClinical and experimental allergy : journal of the British Society for Allergy and Clinical Immunology
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Decoding the Folding of Burkholderia glumae Lipase: Folding Intermediates En Route to Kinetic Stability

2012

The lipase produced by Burkholderia glumae folds spontaneously into an inactive near-native state and requires a periplasmic chaperone to reach its final active and secretion-competent fold. The B. glumae lipase-specific foldase (Lif) is classified as a member of the steric-chaperone family of which the propeptides of alpha-lytic protease and subtilisin are the best known representatives. Steric chaperones play a key role in conferring kinetic stability to proteins. However, until present there was no solid experimental evidence that Lif-dependent lipases are kinetically trapped enzymes. By combining thermal denaturation studies with proteolytic resistance experiments and the description of…

Macromolecular AssembliesProtein StructureProtein FoldingBurkholderiaProtein ConformationStereochemistryBiophysicslcsh:MedicineBiochemistryProtein Chemistrybacterial lipasemolten globuleBacterial ProteinsNative stateBurkholderia glumaeLipaseProtein Interactionslcsh:ScienceBiologyMultidisciplinarybiologylipase-specific foldasePhysicslcsh:RSubtilisinProteinsLipasebiology.organism_classificationMolten globuleEnzymesChaperone ProteinsKineticsBiochemistryChaperone (protein)Enzyme StructureProteolysisFoldasebiology.proteinlcsh:Qsteric chaperoneProtein foldingnear-native folding intermediateResearch ArticleMolecular Chaperones
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5-Methoxyuridine, a new modified constituent in tRNAs of Bacillaceae.

1976

Magnetic Resonance SpectroscopyBiophysicsBacillusBacillus subtilisMass spectrometryBiochemistryMass Spectrometrychemistry.chemical_compoundRNA TransferSpecies SpecificityStructural BiologyGeneticsMolecular BiologyUridineBacillus (shape)BacillaceaebiologyCell BiologyNuclear magnetic resonance spectroscopyRibonucleotidesbiology.organism_classificationChromatography Ion ExchangeUridinechemistryBiochemistrySpectrophotometry UltravioletBacillus subtilisFEBS letters
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