Search results for "sequence data"

showing 10 items of 1952 documents

A new method of anomeric protection and activation based on the conversion of glycosyl azides into glycosyl fluorides

1993

Glycosyl azides provide reliable anomeric protection stable to conditions for hydrolytic removal of ester groups, for reductive opening or release of acetalic diol protection, for the introduction of ether-type protection, and for glycosylation processes. The utility of this anomeric protection is further enhanced as glycosyl azides may be converted into glycosyl fluorides, which can be activated for glycosylation reactions. To this end, glycosyl azides have been subjected to 1,3-dipolar cycloaddition with di-tert-butyl acetylenedicarboxylate. On treatment with hydrogen fluoride-pyridine complex the N-glycosyl triazole derivatives directly give glycosyl fluorides.

AzidesMagnetic Resonance Spectroscopyanimal structuresAnomerGlycosylationOptical RotationMolecular Sequence DataCarbohydrate synthesismacromolecular substancesBiochemistryKoenigs–Knorr reactionAnalytical ChemistryFluoridesStructure-Activity Relationshipchemistry.chemical_compoundCarbohydrate ConformationOrganic chemistryGlycosylGlycosidesGlycosyl donorMolecular StructureOrganic ChemistryChemical glycosylationGlycosyl acceptorGeneral Medicinecarbohydrates (lipids)Carbohydrate Sequencechemistrylipids (amino acids peptides and proteins)Carbohydrate Research
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Disentangling the rhizosphere effect on nitrate reducers and denitrifiers: insight into the role of root exudates.

2008

International audience; To determine to which extent root-derived carbon contributes to the effects of plants on nitrate reducers and denitrifiers, four solutions containing different proportions of sugar, organic acids and amino acids mimicking maize root exudates were added daily to soil microcosms at a concentration of 150 μg C g−1 of soil. Water-amended soils were used as controls. After 1 month, the size and structure of the nitrate reducer and denitrifier communities were analysed using the narG and napA, and the nirK, nirS and nosZ genes as molecular markers respectively. Addition of artificial root exudates (ARE) did not strongly affect the structure or the density of nitrate reduce…

BACTERIAL COMMUNITY STRUCTURE REAL-TIME PCRDNA BacterialDenitrificationMolecular Sequence DataDIVERSITYBiologyGENETIC-STRUCTURENIRKNitrate reductaseMicrobiologyPlant RootsZea mays03 medical and health scienceschemistry.chemical_compoundNitrateBacterial ProteinsBotanyPLANTSSugarEcology Evolution Behavior and SystematicsNitritesSoil Microbiology030304 developmental biology2. Zero hunger0303 health sciencesRhizosphereNitratesBacteria04 agricultural and veterinary sciencesBiodiversitySequence Analysis DNA6. Clean waterCarbonSOIL[SDV.MP]Life Sciences [q-bio]/Microbiology and Parasitologychemistry13. Climate actionEnvironmental chemistrySoil water040103 agronomy & agriculture0401 agriculture forestry and fisheriesComposition (visual arts)MicrocosmOxidoreductasesOxidation-ReductionMAIZENOSZ GENESEnvironmental microbiology
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Vibrio agarivorans sp. nov., a novel agarolytic marine bacterium.

2002

It is proposed that the new Vibrio species Vibrio agarivorans accommodates two agarolytic, halophilic, fermentative bacterial strains isolated from Mediterranean sea water. The cells were gram-negative, oxidase-positive, polarly flagellated bacilli that fermented glucose without gas production and that produced no decarboxylases. They used a wide range of compounds as sole carbon and energy sources. The DNA G+C content was 44.8 mol%. Phylogenetic analysis based on complete 16S and 23S rDNA sequences revealed that the strains belong to the gamma-Proteobacteria, and are specifically related to Vibrio species. Their nearest relatives were species of the Vibrio fischeri group, sharing 16S rDNA …

BacilliSequence analysisMolecular Sequence DataGeneral MedicineSequence Analysis DNABiology16S ribosomal RNAbiology.organism_classificationMicrobiologyDNA RibosomalVibrioHalophileMicrobiologyAgarRNA Ribosomal 23SBiochemistryVibrionaceaeRNA Ribosomal 16SMediterranean SeaSeawaterEnergy sourceEcology Evolution Behavior and SystematicsBacteriaPhylogenyVibrioInternational journal of systematic and evolutionary microbiology
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Bacterial sensor kinases using Fe–S cluster binding PAS or GAF domains for O2sensing

2012

[4Fe-4S](2+) clusters are used by very diverse types of bacterial sensors for response to oxygen, including DNA-binding proteins of the CRP/FNR family and sensor kinases like NreB. In NreB the cluster is bound by an input domain of the PAS type. The [4Fe-4S](2+) cluster of NreB responds to O(2) by degradation to a [2Fe-2S](2+) cluster which is labile and decomposes. NreB constitutes together with AirS the NreB/AirS family of bacterial sensor kinases that contain PAS or GAF domains for binding of [4Fe-4S](2+) or [2Fe-2S](2+) clusters and oxygen sensing. The NreB/AirS family is related to the FixL sensor kinases that use hemeB binding PAS domains for oxygen sensing.

BacteriaKinaseStereochemistryChemistryIronOxygen metabolismMolecular Sequence DataPhosphotransferasesO2 sensingBioinformaticsProtein Structure TertiaryOxygenInorganic ChemistryProtein structureCluster (physics)Amino Acid SequencePeptide sequenceOxygen sensingSulfurDalton Trans.
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Stimulated and unstimulated saliva samples have significantly different bacterial profiles

2018

Epidemiological studies use saliva on a regular basis as a non-invasive and easy-to-take sample, which is assumed to be a microbial representative of the oral cavity ecosystem. However, comparative studies between different kinds of saliva samples normally used in microbial studies are scarce. The aim of the current study was to compare oral microbiota composition between two different saliva samples collected simultaneously: non-stimulated saliva with paper points and stimulated saliva collected after chewing paraffin gum. DNA was extracted from saliva samples of ten individuals, then analyzed by 16S rRNA pyrosequencing to describe bacterial diversity. The results demonstrate significant d…

Bacterial DiseasesMale0301 basic medicineSalivaPhysiologylcsh:MedicineMicrobiologiaPathology and Laboratory MedicineOral cavityDatabase and Informatics Methodsfluids and secretions0302 clinical medicineOral DiseasesCariesMedicine and Health SciencesFood sciencelcsh:ScienceChildMultidisciplinaryGenomicsBody FluidsBacterial PathogensInfectious Diseasesmedicine.anatomical_structureMedical MicrobiologyParaffinFemaleAnatomyPathogensSequence AnalysisResearch ArticleAdolescentBioinformaticsOral MedicineSequence DatabasesMicrobial GenomicsBiologyResearch and Analysis MethodsDental plaqueMicrobiologyBuccal mucosa03 medical and health sciencesOral Microbiotastomatognathic systemTongueGeneticsmedicineHumansEpidemiologiaSalivaMicrobial PathogensBacteriaBocalcsh:ROrganismsBiology and Life SciencesStreptococcus030206 dentistrymedicine.disease16S ribosomal RNAstomatognathic diseasesBiological Databases030104 developmental biologyEstomatologiaPyrosequencinglcsh:QMicrobiomePLOS ONE
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Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin: prototypes of pore-forming bacterial cytolysins.

1996

Staphylococcal alpha-toxin, streptolysin-O, and Escherichia coli hemolysin are well-studied prototypes of pore-forming bacterial cytotoxins. Each is produced as a water-soluble single-chain polypeptide that inserts into target membranes to form aqueous transmembrane pores. This review will compare properties of the three toxin prototypes, highlighting the similarities and also the differences in their structure, mode of binding, mechanism of pore formation, and the responses they elicit in target cells. Pore-forming toxins represent the most potent and versatile weapons with which invading microbes damage the host macroorganism.

Bacterial ToxinsLipid BilayersMolecular Sequence Datamedicine.disease_causeBiochemistryMicrobiologyMicrobiologyHemolysin ProteinsBacterial ProteinsEscherichiaGeneticsmedicineAnimalsHumansAmino Acid SequenceMolecular BiologyEscherichia colibiologyToxinEscherichia coli ProteinsCell MembraneHemolysinGeneral Medicinebiology.organism_classificationEnterobacteriaceaeBiochemistryStreptolysinsStreptolysinCytolysinExotoxinArchives of microbiology
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Delineation of the catalytic domain of Clostridium difficile toxin B-10463 to an enzymatically active N-terminal 467 amino acid fragment.

2006

Abstract In an attempt to directly approach the postulated toxic domain of Clostridium difficile 's TcdB-10463, eight subclones of different size and locations in the N-terminal third of the toxin were generated. Expression of these toxin fragments was checked in Western blots and the enzymatic activity of the expressed proteins was analyzed by glucosylating Ras related small GTP-binding proteins. Two polypeptides of 875 aa (TcdBc1–3) and 557 aa (TcdBc1-H) glucosylated their targets Rho, Rac and Cdc42 with the same activity and specificity as the holotoxin. In comparison 516 aa (TcdBc1-N) and 467 aa (TcdBc1-A) protein fragments exhibited highly reduced activity, while Tcdc1 and TcdB2–3 (aa …

Bacterial ToxinsMolecular Sequence DataClostridium difficile toxin Bmedicine.disease_causeMicrobiologyStructure-Activity RelationshipGTP-binding protein regulatorsClostridiumBacterial ProteinsGeneticsmedicineMolecular Biologychemistry.chemical_classificationBinding SitesbiologyBase SequenceToxinbiology.organism_classificationMolecular biologyPeptide FragmentsRecombinant ProteinsAmino acidEnzymechemistryCdc42 GTP-Binding ProteinBiochemistryGlucosyltransferasesbiology.proteinGlucosyltransferaseFEMS microbiology letters
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Evidence for a modular structure of the homologous repetitive C-terminal carbohydrate-binding sites of Clostridium difficile toxins and Streptococcus…

1992

The homologous C-terminal repeats of Clostridium difficile toxins (ToxA and ToxB) and streptococcal glucosyltransferases appear to mediate protein-carbohydrate interactions at cellular binding sites with sugar moieties as substrates. A consensus sequence of 134 repeating units from gram-positive bacteria indicates that these repeats have a modular design with (i) a stretch of aromatic amino acids proposed to be involved in the primary carbohydrate-protein interaction, (ii) an amplification of this interaction by repetition of the respective sequences, and (iii) a second domain, not characterized, that is responsible for carbohydrate specificity.

Bacterial ToxinsMolecular Sequence DataEnterotoxinMicrobiologyMicrobiologyStreptococcus mutanschemistry.chemical_compoundEnterotoxinsGlucosyltransferasesBacterial ProteinsGlycosyltransferaseConsensus SequenceConsensus sequenceAromatic amino acidsAmino Acid SequenceBinding siteMolecular BiologyPeptide sequenceBinding SitesbiologySequence Homology Amino AcidClostridioides difficileCytotoxinsClostridium difficilechemistryBiochemistryGlucosyltransferasesbiology.proteinCarbohydrate MetabolismResearch ArticleJournal of bacteriology
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Shared Binding Sites in Lepidoptera for Bacillus thuringiensis Cry1Ja and Cry1A Toxins

2001

ABSTRACT Bacillus thuringiensis toxins act by binding to specific target sites in the insect midgut epithelial membrane. The best-known mechanism of resistance to B. thuringiensis toxins is reduced binding to target sites. Because alteration of a binding site shared by several toxins may cause resistance to all of them, knowledge of which toxins share binding sites is useful for predicting cross-resistance. Conversely, cross-resistance among toxins suggests that the toxins share a binding site. At least two strains of diamondback moth ( Plutella xylostella ) with resistance to Cry1A toxins and reduced binding of Cry1A toxins have strong cross-resistance to Cry1Ja. Thus, we hypothesized that…

Bacterial ToxinsMolecular Sequence DataSpodopteraBinding CompetitiveApplied Microbiology and BiotechnologyMicrobiologyInsecticide ResistanceHemolysin ProteinsBacterial ProteinsBacillus thuringiensisBotanyInvertebrate MicrobiologyAnimalsAmino Acid SequenceBinding siteBinding SitesDiamondback mothBacillus thuringiensis ToxinsEcologybiologyHeliothis virescensfungibiology.organism_classificationEndotoxinsLepidopteraPlutellidaeCry1AcLarvaNoctuidaeFood ScienceBiotechnologyApplied and Environmental Microbiology
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Downregulation of a Chitin Deacetylase-Like Protein in Response to Baculovirus Infection and Its Application for Improving Baculovirus Infectivity

2009

ABSTRACT Several expressed sequence tags (ESTs) with homology to chitin deacetylase-like protein (CDA) were selected from a group of Helicoverpa armigera genes whose expression changed after infection with H. armigera single nucleopolyhedrovirus (HearNPV). Some of these ESTs coded for a midgut protein containing a chitin deacetylase domain (CDAD). The expressed protein, HaCDA5a, did not show chitin deacetylase activity, but it showed a strong affinity for binding to chitin. Sequence analysis showed the lack of any chitin binding domain, described for all currently known peritrophic membrane (PM) proteins. HaCDA5a has previously been detected in the H. armigera PM. Such localization, togethe…

BaculoviridaeExpressed Sequence TagvirusesMolecular Sequence DataImmunologyDown-RegulationChitinMothMothsSpodopteraSpodopteraHelicoverpa armigeraMicrobiologyAmidohydrolasesMicrobiologychemistry.chemical_compoundChitinDownregulation and upregulationChitin bindingVirologyAnimalsAmino Acid SequenceCells CulturedPhylogenyOligonucleotide Array Sequence AnalysisExpressed Sequence TagsAmidohydrolaseInfectivitySequence Homology Amino AcidbiologyAnimalOligonucleotide Array Sequence AnalysiGene Expression ProfilingfungiSequence Analysis DNAbiology.organism_classificationVirologyIsoenzymeGenome Replication and Regulation of Viral Gene ExpressionChitin deacetylaseIsoenzymeschemistryInsect ScienceBaculoviridaeSequence AlignmentJournal of Virology
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