Search results for "bacterial protein"

showing 10 items of 616 documents

The Proteome and Lipidome of Synechocystis sp. PCC 6803 Cells Grown under Light-Activated Heterotrophic Conditions*

2015

Cyanobacteria are photoautotrophic prokaryotes with a plant-like photosynthetic machinery. Because of their short generation times, the ease of their genetic manipulation, and the limited size of their genome and proteome, cyanobacteria are popular model organisms for photosynthetic research. Although the principal mechanisms of photosynthesis are well-known, much less is known about the biogenesis of the thylakoid membrane, hosting the components of the photosynthetic, and respiratory electron transport chain in cyanobacteria. Here we present a detailed proteome analysis of the important model and host organism Synechocystis sp. PCC 6803 under light-activated heterotrophic growth condition…

CyanobacteriaProtein FoldingProteomePhotosynthesisThylakoidsBiochemistryMass SpectrometryAnalytical ChemistryRespiratory electron transport chainMembrane LipidsBacterial ProteinsMolecular BiologybiologyResearchSynechocystisLipidomebiology.organism_classificationCarbonOxidative StressPhototrophic ProcessesMembraneBiochemistryThylakoidProteomeBiogenesisChromatography LiquidMolecular & Cellular Proteomics
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The Biosynthesis of Rare Homo-Amino Acid Containing Variants of Microcystin by a Benthic Cyanobacterium

2019

Microcystins are a family of chemically diverse hepatotoxins produced by distantly related cyanobacteria and are potent inhibitors of eukaryotic protein phosphatases 1 and 2A. Here we provide evidence for the biosynthesis of rare variants of microcystin that contain a selection of homo-amino acids by the benthic cyanobacterium Phormidium sp. LP904c. This strain produces at least 16 microcystin chemical variants many of which contain homophenylalanine or homotyrosine. We retrieved the complete 54.2 kb microcystin (mcy) gene cluster from a draft genome assembly. Analysis of the substrate specificity of McyB1 and McyC adenylation domain binding pockets revealed divergent substrate specificity …

CyanobacteriamassaspektrometriaMicrocystinstoksiinitPharmaceutical ScienceMicrocystinPlanktothrixcyanobacteriaArticlebiosynteesi03 medical and health scienceschemistry.chemical_compoundBiosynthesisBacterial ProteinsDrug DiscoveryGene clusterpolycyclic compoundspolyketide synthase (PKS)Protein Interaction Domains and MotifsAmino Acid SequenceAmino AcidssyanobakteeritPharmacology Toxicology and Pharmaceutics (miscellaneous)Genelcsh:QH301-705.5Phylogeny030304 developmental biologymass spectrometrychemistry.chemical_classification0303 health sciencesbiology030302 biochemistry & molecular biologyta1182Sequence Analysis DNAbiology.organism_classificationAmino acidEnzymechemistryBiochemistrylcsh:Biology (General)adenylation domainGenes BacterialMultigene Familynonribosomal peptide synthetase (NRPS)hepatotoxinMarine Drugs
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Changes in membrane lipid composition in ethanol- and acid-adapted Oenococcus oeni cells: characterization of the cfa gene by heterologous complement…

2008

International audience; Cyclopropane fatty acid (CFA) synthesis was investigated in Oenococcus oeni. The data obtained demonstrated that acid-grown cells or cells harvested in the stationary growth phase showed changes in fatty acid composition similar to those of ethanol-grown cells. An increase of the CFA content and a decrease of the oleic acid content were observed. The biosynthesis of CFAs from unsaturated fatty acid phospholipids is catalysed by CFA synthases. Quantitative real-time-PCR experiments were performed on the cfa gene of O. oeni, which encodes a putative CFA synthase. The level of cfa transcripts increased when cells were harvested in stationary phase and when cells were gr…

CyclopropanesMESH: Hydrogen-Ion ConcentrationTranscription GeneticMESH: Gram-Positive Coccimedicine.disease_causechemistry.chemical_compoundMESH: CyclopropanesCloning MolecularMESH: Bacterial ProteinsOenococcus oeni0303 health sciencesMESH: Gene Expression Regulation BacterialMESH: Genetic Complementation TestbiologyStrain (chemistry)MESH: Escherichia coliFatty AcidsHydrogen-Ion ConcentrationMESH: Fatty AcidsGram-Positive CocciComplementationRNA BacterialBiochemistryMESH: RNA BacterialMESH: EthanolMESH: Sequence AlignmentMicrobiologycomplex mixturesMembrane Lipids03 medical and health sciencesBacterial ProteinsMESH: MethyltransferasesEscherichia colimedicineMESH: Cloning Molecular[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyCyclopropane fatty acidEthanol metabolismEscherichia coliUnsaturated fatty acid030304 developmental biologyEthanol030306 microbiologyMESH: Transcription GeneticGenetic Complementation TestMESH: Oleic AcidGene Expression Regulation BacterialMethyltransferasesbiology.organism_classificationOleic acidchemistryMESH: Membrane LipidsSequence AlignmentOleic Acid
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Ferric-reductase activities in Vibrio vulnificus biotypes 1 and 2.

1999

In this paper, the ferric-reductase activities of Vibrio vulnificus were investigated. This species comprises two biotypes pathogenic for humans and eels that are able to express different mechanisms for iron acquisition. All strains of both biotypes used in this study were able to reduce ferric citrate, irrespective of the iron levels in the growth medium. Some variation in the degree of reduction was observed among the strains, with the highest values corresponding to one acapsulated environmental strain of biotype 1. When cell fractions were tested, only those from periplasm and cytoplasm showed reductase activity whereas no activity was detected in membranes. Low temperatures inhibited …

CytoplasmTime FactorsFMN ReductaseIronVibrio vulnificusReductaseMicrobiologyFerric CompoundsMicrobiologychemistry.chemical_compoundBacterial ProteinsVibrionaceaeGeneticsAnimalsHumansNADH NADPH OxidoreductasesMolecular BiologyVibrioGrowth mediumEelsbiologyStrain (chemistry)Cell MembranePeriplasmic spacebiology.organism_classificationCulture MediachemistryBiochemistryCytoplasmPeriplasmbacteriaElectrophoresis Polyacrylamide GelBacteriaFEMS microbiology letters
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Deinococcus radiodurans' SRA-HNH domain containing protein Shp (Dr1533) is involved in faithful genome inheritance maintenance following DNA damage

2018

WOS:000452343100012; International audience; Background: Deinococcus radiodurans R1 (DR) survives conditions of extreme desiccation, irradiation and exposure to genotoxic chemicals, due to efficient DNA breaks repair, also through Mn2+ protection of DNA repair enzymes. Methods: Possible annotated domains of the DR1533 locus protein (Shp) were searched by bioinformatic analysis. The gene was cloned and expressed as fusion protein. Band-shift assays of Shp or the SRA and HNH domains were performed on oligonucleotides, genomic DNA from E. coif and DR. slip knock-out mutant was generated by homologous recombination with a kanamycin resistance cassette. Results: DR1533 contains an N-terminal SRA…

DNA RepairDNA cytosine-methylation; DNA damage; DR1533 locus; Genotoxic agents; Mn2+; SRA domain; Biophysics; Biochemistry; Molecular BiologyGenotoxic agents[SDV]Life Sciences [q-bio]DNA cytosine-methylationperspectiveSettore BIO/19 - Microbiologia GeneraleBiochemistrychemistry.chemical_compound0302 clinical medicineKanamycinCloning Molecularcytosine0303 health sciencesDR1533 locusbiologyChemistryGenotoxic agentuhrf1Mn(2+)Mn2+SRA domainDeinococcusrecognitionmanganese(ii)DNA BacterialDNA damageDNA repairoxidationUbiquitin-Protein LigasesBiophysicsSettore BIO/11 - Biologia Molecolareresistance03 medical and health sciencesBacterial ProteinsProtein DomainsDR1533 locuDrug Resistance BacterialEscherichia coliHumansfeaturesAmino Acid SequenceGeneMolecular Biology030304 developmental biologyOligonucleotideComputational BiologyDeinococcus radioduransDNA Methylationbiology.organism_classificationMolecular biologygenomic DNArepairMutationCCAAT-Enhancer-Binding ProteinsDNA damageHomologous recombination030217 neurology & neurosurgeryDNAGenome BacterialMutagens
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Mechanisms of quinolone resistance in Aeromonas species isolated from humans, water and eels.

2009

Mechanisms of resistance were determined in 33 quinolone-resistant isolates of the species Aeromonas hydrophila, Aeromonas caviae, Aeromonas media, Aeromonas salmonicida, Aeromonas popoffii and Aeromonas veronii, recovered from humans, freshwater and eels. The quinolone resistance-determining regions (QRDRs) of gyrA and parC genes were sequenced in these resistant strains, as well as in 8 quinolone-sensitive Aeromonas used as controls. All quinolone-resistant Aeromonas carried point mutations in the gyrA QRDR at codon 83, respectively giving rise to substitutions Ser(83)-->Ile (32 strains) or Ser(83)-->Val (1 strain). Almost half of these isolates (48%) carried additional point mutations in…

DNA Topoisomerase IVDNA BacterialAeromonas caviaemedicine.drug_classDNA Mutational AnalysisMutation MissenseDrug resistanceMicrobial Sensitivity TestsQuinolonesMicrobiologyMicrobiologyBacterial ProteinsDrug Resistance BacterialmedicineAnimalsHumansPoint MutationMolecular BiologyEelsbiologyGeneral MedicineSequence Analysis DNAbiochemical phenomena metabolism and nutritionQuinolonebiology.organism_classificationAnti-Bacterial AgentsAeromonas hydrophilaAeromonas salmonicidaAeromonasAmino Acid SubstitutionDNA GyraseAeromonas mediaAeromonasGram-Negative Bacterial InfectionsWater MicrobiologyAeromonas veroniiResearch in microbiology
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Spontaneous Quinolone Resistance in the Zoonotic Serovar of Vibrio vulnificus

2009

ABSTRACT This work demonstrates that Vibrio vulnificus biotype 2, serovar E, an eel pathogen able to infect humans, can become resistant to quinolone by specific mutations in gyrA (substitution of isoleucine for serine at position 83) and to some fluoroquinolones by additional mutations in parC (substitution of lysine for serine at position 85). Thus, to avoid the selection of resistant strains that are potentially pathogenic for humans, antibiotics other than quinolones must be used to treat vibriosis on farms.

DNA Topoisomerase IVDNA BacterialSerotypeBiologiamedicine.drug_classMolecular Sequence DataAntibioticsMutation MissenseMicrobiologiaPublic Health MicrobiologyVibrio vulnificusQuinolonesApplied Microbiology and BiotechnologyDNA gyraseMicrobiologyBacterial ProteinsVibrionaceaeDrug Resistance BacterialmedicineAnimalsVibrio vulnificusPathogenEelsEcologybiologySequence Analysis DNAbiology.organism_classificationQuinoloneVirologyAnti-Bacterial AgentsDNA GyrasebacteriaBacteriaFood ScienceBiotechnologyApplied and Environmental Microbiology
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Selection of amine-oxidizing dairy lactic acid bacteria and identification of the enzyme and gene involved in the decrease of biogenic amines

2016

ABSTRACT Accumulation of biogenic amines (BAs) in cheese and other foods is a matter of public health concern. The aim of this study was to identify the enzyme activities responsible for BA degradation in lactic acid bacteria which were previously isolated from traditional Sicilian and Apulian cheeses. The selected strains would control the concentration of BAs during cheese manufacture. First, 431 isolates not showing genes encoding the decarboxylases responsible for BA formation were selected using PCR-based methods. Ninety-four out of the 431 isolates degraded BAs (2-phenylethylamine, cadaverine, histamine, putrescine, spermine, spermidine, tyramine, or tryptamine) during cultivation on …

DNA Bacterial0301 basic medicineBiogenic AminesLactobacillus caseiBiotechnology; Food Science; Applied Microbiology and Biotechnology; EcologyCarboxy-Lyases030106 microbiologyApplied Microbiology and BiotechnologyMicrobiology03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsCheeseRNA Ribosomal 16SFood microbiologyCadaverineBacteriaBase SequencebiologyEcologyLactococcus lactisfood and beveragesStreptococcusTyraminebiology.organism_classificationLactic acidLactobacillus030104 developmental biologychemistryWeissellaFood MicrobiologyPutrescineOxidoreductasesEnterococcusBacteriaBiotechnologyFood ScienceSettore AGR/16 - Microbiologia Agraria
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Evaluation of the DNA microarray “AMR Direct Flow Chip Kit” for detection of antimicrobial resistance genes from Gram-positive and Gram-negative bact…

2019

Abstract Introduction The AMR Direct Flow Chip assay allows the simultaneous detection of a large variety of antibiotic resistance genetic markers. To assess this kit's performance, we use isolated colonies as starting material. The assay has been approved by the European Economic Area as a suitable device for in vitro diagnosis (CE IVD) using clinical specimens. Methods A total of 210 bacterial isolates harbouring either one or more antimicrobial resistance genes including plasmid-encoded extended-spectrum β-lactamases (SHV, CTX-M) and carbapenemases (GES, SME, KPC, NMC/IMI, SIM, GIM, SPM, NDM, VIM, IMP, and OXA), mecA, vanA and vanB, and 30 controls were included. Results The assay displa…

DNA Bacterial0301 basic medicineMicrobiology (medical)030106 microbiologyGram-Positive BacteriaSensitivity and Specificitybeta-Lactam Resistancebeta-LactamasesMicrobiology03 medical and health sciences0302 clinical medicineAntibiotic resistanceBacterial ProteinsVancomycinDrug Resistance Multiple BacterialGram-Negative Bacteriapolycyclic compoundsmedicineHumans030212 general & internal medicineGeneGram-Positive Bacterial InfectionsOligonucleotide Array Sequence AnalysisGrambiologyDrug Resistance Microbialbiochemical phenomena metabolism and nutritionbacterial infections and mycosesbiology.organism_classificationIn vitroGenes BacterialGenetic markerVancomycinReagent Kits DiagnosticDNA microarrayGram-Negative Bacterial InfectionsBacteriamedicine.drugEnfermedades infecciosas y microbiologia clinica (English ed.)
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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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