Search results for "bacteri"

showing 10 items of 5466 documents

Marinifilum flexuosum sp. nov., a new Bacteroidetes isolated from coastal Mediterranean Sea water and emended description of the genus Marinifilum Na…

2012

Abstract A facultatively anaerobe, moderately halophilic, Gram-negative, filamentous, non motile and unpigmented bacterium, designated M30 T , was isolated from coastal Mediterranean Sea water in Valencia, Spain. Phylogenetic analysis based on 16S rRNA sequences placed this strain in the phylum “ Bacteroidetes ” with Marinifilum fragile JC2469 T as its closest relative with 97% sequence similarity. Average nucleotide identity (ANI) values between both strains were far below the 95% threshold value for species delineation (about 89% using BLAST and about 90% using MUMmer). A comprehensive polyphasic study, including morphological, biochemical, physiological, chemotaxonomic and phylogenetic d…

Strain (chemistry)Phylogenetic treePhylumBacteroidetesMolecular Sequence DataBacteroidetesBiologybiology.organism_classification16S ribosomal RNAApplied Microbiology and BiotechnologyMicrobiologyHalophileMicrobiologyBacterial Typing TechniquesMediterranean seaGenusRNA Ribosomal 16SBotanyMediterranean SeaSeawaterEcology Evolution Behavior and SystematicsPhylogenySystematic and applied microbiology
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Methane-derived carbonate conduits from the late Aptian of Salinac (Marne Bleues, Vocontian Basin, France): Petrology and biosignatures

2015

Abstract Peculiar carbonate bodies occur in distinct marl layers of the Marnes Bleues Formation (Aptian–Albian, Vocontian Basin, Southern France). The carbonate conduits exhibit pipe- or sausage-like forms and a central channel. Their sizes range between 30 and 60 cm in length and 5–10 cm in diameter. The conduit carbonates consist of automicrite authigenically formed within the sediment. Millimeter-sized aggregates of framboidal pyrite are abundant within the conduit automicrites, probably representing former colonies of sulfate reducing bacteria. The central channel reflects former pathways of reduced fluids in the carbonate conduit. Ni-enrichments at the margins of the central cavity are…

StratigraphyMineralogyGeologyAuthigenicengineering.materialOceanographychemistry.chemical_compoundGeophysicschemistry13. Climate actionIsotopes of carbonAnaerobic oxidation of methaneMarlengineeringCarbonateEconomic GeologyPyriteSulfateSulfate-reducing bacteriaGeologyMarine and Petroleum Geology
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High-resolution crystal structure of an avidin-related protein: insight into high-affinity biotin binding and protein stability.

2004

The chicken avidin gene belongs to an extended gene family encoding seven avidin-related genes (AVRs), of which only avidin is expressed in the chicken. The sequences of AVR4 and AVR5 are identical and the common protein (AVR4) has been expressed both in insect and bacterial systems. The recombinant proteins are similarly hyperthermostable and bind biotin with similarly high affinities. AVR4 was crystallized in the apo and biotin-complexed forms and their structures were determined at high resolution. Its tertiary and quaternary structures are very similar to those of avidin and streptavidin. Its biotin-binding site shows only a few alterations compared with those of avidin and streptavidin…

StreptavidinBiotin bindingHot TemperatureBiotinBiologylaw.inventionchemistry.chemical_compoundBiotinStructural BiologylawAnimalsProtein Structure QuaternaryThermostabilityBacteriaHydrogen BondingGeneral MedicineAvidinAffinitiesBiochemistrychemistryBiotinylationData Interpretation StatisticalBiophysicsRecombinant DNAbiology.proteinStreptavidinCrystallizationBaculoviridaeChickensAvidinProtein BindingActa crystallographica. Section D, Biological crystallography
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Interaction between biotin lipids and streptavidin in monolayers: formation of oriented two-dimensional protein domains induced by surface recognitio…

1989

Highly specific ligand-receptor interactions generally characterize surface recognition reactions. Such processes can be simulated by streptavidin-biotin-specific binding. Biotin lipids have thus been synthesized, and their interaction with streptavidin (or avidin) at the air-water interface was directly shown by measurement of surface pressure isotherms and fluorescence microscopy. These proteins interact with the biotin lipid monolayer via specific binding or nonspecific adsorption. Both phenomena were clearly distinguished by use of the inactivated form of streptavidin. The binding of fluorescein-labeled streptavidin to monolayers was also directly observed by fluorescence microscopy. Th…

StreptavidinChemical PhenomenaSurface PropertiesProtein domainBiotinBiochemistrychemistry.chemical_compoundBiotinBacterial ProteinsMonolayerFluorescence microscopebiologyChemistryChemistry PhysicalPhosphatidylethanolaminestechnology industry and agricultureMembranes ArtificialHydrogen-Ion ConcentrationAvidinFluorescenceLipidsSpectrometry FluorescenceSolubilityBiotinylationbiology.proteinBiophysicsSpectrophotometry UltravioletStreptavidinAvidinBiochemistry
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(Strept)avidin as host for biotinylated coordination complexes: stability, chiral discrimination, and cooperativity

2005

Incorporation of a biotinylated ruthenium tris(bipyridine) [Ru(bpy)₂(Biot-bpy)]²⁺ (1) in either avidin or streptavidin-(strept)avidin-can be conveniently followed by circular dichroism spectroscopy. To determine the stepwise association constants, cooperativity, and chiral discrimination properties, diastereopure (Λ and δ)-1 species were synthesized and incorporated in tetrameric (strept)avidin to afford (δ-[Ru(bpy)₂(Biot-bpy)]²⁺)x⊂avidin, (Λ- [Ru(bpy)₂(Biot-bpy)]²⁺)x⊂avidin, (δ-[Ru(bpy)₂(Biot- bpy)]²⁺)x⊂streptavidin, and (Λ-[Ru(bpy)₂(Biot-bpy)]²⁺) x⊂streptavidin (x = 1-4) For these four systems, the overall stability constants are log β₄ = 28.6, 30.3, 36.2, and 36.4, respectively. Critical…

StreptavidinCircular dichroismProtein ConformationStereochemistryBiotinchemistry.chemical_elementCooperativity010402 general chemistry01 natural sciencesInorganic ChemistryStructure-Activity RelationshipBipyridinechemistry.chemical_compound22'-DipyridylBacterial ProteinsBiotinCoordination ComplexesBiotinylation[CHIM.COOR]Chemical Sciences/Coordination chemistryPhysical and Theoretical ChemistryComputingMilieux_MISCELLANEOUSMolecular Structurebiology010405 organic chemistry[ CHIM.COOR ] Chemical Sciences/Coordination chemistryAvidinProtein Structure Tertiary0104 chemical sciencesRuthenium[CHIM.THEO]Chemical Sciences/Theoretical and/or physical chemistryCrystallographychemistryBiotinylation[ CHIM.THEO ] Chemical Sciences/Theoretical and/or physical chemistrybiology.proteinStreptavidinAvidin
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X-ray diffraction of a protein crystal anchored at the air/water interface

1995

We report the first successful in situ x-ray diffraction experiment with a 2D protein array at the lipid/water interface and demonstrate that the order can be controlled via lateral pressure or density. A protein (streptavidin) was bound to a monolayer of biotinylated lipid at the air/water interface, and diffraction of the protein layer could be measured to many orders. Compression of the monolayer changed the diffraction pattern drastically, indicating that the protein structure can be strongly influenced by external parameters like lateral pressure or density. From the width of the peaks, we find that aggregates consisting of as few as 100 monomers contribute to the diffraction. This ind…

StreptavidinDiffractionProtein ConformationAnalytical chemistryBiophysicsCrystallography X-RayBiophysical Phenomenalaw.inventionCrystalchemistry.chemical_compoundProtein structureBacterial ProteinslawMonolayerCrystallizationPhospholipidsGrazing incidence diffractionMolecular StructureAirfood and beveragesProteinsWaterCrystallographychemistryX-ray crystallographyStreptavidinResearch ArticleBiophysical Journal
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Formation of protein multilayers and their competitive replacement based on self-assembled biotinylated phospholipids.

1994

Based on specific recognition processes the build-up of protein multilayers was achieved using streptavidin layers as a docking matrix. For this purpose, streptavidin was organized at biotin-containing monolayers, liposomes, and self-assembled layers on gold. Thus, mixed double and triple layers of streptavidin, Con A, Fab fragments, and hormones were prepared and characterized by fluorescence microscopy and plasmon spectroscopy. Using biotin analogues with lower binding constants several cycles of multilayer formation followed by competitive replacement could be achieved.

StreptavidinLiposomeSurface Propertiestechnology industry and agricultureBiomedical EngineeringBiophysicsBiotinProteinsBioengineeringBinding CompetitiveBiomaterialsCrystallographychemistry.chemical_compoundMolecular recognitionBiotinchemistryBacterial ProteinsDocking (molecular)BiotinylationMonolayerFluorescence microscopeStreptavidinPhospholipidsJournal of biomaterials science. Polymer edition
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The Sensor Kinase DctS Forms a Tripartite Sensor Unit with DctB and DctA for Sensing C4-Dicarboxylates in Bacillus subtilis

2013

The DctSR two-component system of Bacillus subtilis controls the expression of the aerobic C4-dicarboxylate transporter DctA. Deletion of DctA leads to an increased dctA expression. The inactivation of DctB, an extracellular binding protein, is known to inhibit the expression of dctA. Here, interaction between the sensor kinase DctS and the transporter DctA as well as the binding protein DctB was demonstrated in vivo using streptavidin (Strep) or His protein interaction experiments (mSPINE or mHPINE), and the data suggest that DctA and DctB act as cosensors for DctS. The interaction between DctS and DctB was also confirmed by the bacterial two-hybrid system (BACTH). In contrast, no indicati…

StreptavidinRegulation of gene expressionKinaseBinding proteinMembrane ProteinsTransporterGene Expression Regulation BacterialArticlesPlasma protein bindingBacillus subtilisBiologybiology.organism_classificationMicrobiologyGene Expression Regulation Enzymologicchemistry.chemical_compoundPlasmidBacterial ProteinsBiochemistrychemistryDicarboxylic AcidsCarrier ProteinsMolecular BiologyBacillus subtilisPlasmidsProtein BindingJournal of Bacteriology
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Molecular mechanisms determining the strength of receptor-mediated intermembrane adhesion

1995

The strength of receptor-mediated cell adhesion is directly controlled by the mechanism of cohesive failure between the cell surface and underlying substrate. Unbinding can occur either at the locus of the specific bond or within the bilayer, which results in tearing the hydrophobic anchors from the membrane interior. In this work, the surface force apparatus has been used to investigate the relationship between the receptor-ligand bond affinities and the dominant mechanism of receptor-coupled membrane detachment. The receptors and ligands used in this study were membrane-bound streptavidin and biotin analogs, respectively, with solution affinities ranging over 10 orders of magnitude. With …

StreptavidinStereochemistryLipid BilayersMolecular ConformationBiophysicsReceptors Cell Surface02 engineering and technologyModels BiologicalCell membrane03 medical and health scienceschemistry.chemical_compoundBacterial ProteinsmedicineCell AdhesionAnimalsBond energyLipid bilayer030304 developmental biologyFluorescent Dyes0303 health sciencesThioctic AcidBilayerPhosphatidylethanolaminesCell MembraneSurface forces apparatus021001 nanoscience & nanotechnologyAffinitiesModels StructuralKineticsmedicine.anatomical_structureMembranechemistryBiophysicsStreptavidin0210 nano-technologyAzo CompoundsResearch ArticleBiophysical Journal
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Crystallization and preliminary X-ray analysis of W120K mutant of streptavidin.

2001

Bacterial streptavidin and chicken avidin are homotetrameric proteins that share an exceptionally high affinity towards the vitamin biotin. The biotin-binding sites in both proteins contain a crucial tryptophan residue contributed from an adjacent subunit. This particular tryptophan (W110 in avidin and W120 in streptavidin) plays an important role in both biotin binding and in the quaternary stabilities of the proteins. An intriguing naturally occurring alteration of tryptophan to lysine was previously described in the C-terminal domain of sea-urchin fibropellins, which share a relatively high sequence similarity with avidin and streptavidin. Avidin (Avm-W110K) and streptavidin (Savm-W120K)…

StreptavidinStrep-tagBiotin bindingbiologyProtein ConformationLysineTryptophanTryptophanGeneral MedicineCrystallography X-Raychemistry.chemical_compoundCrystallographyProtein structureBiotinchemistryAmino Acid SubstitutionBacterial ProteinsStructural BiologyBiotinylationMutationbiology.proteinStreptavidinCrystallizationBaculoviridaeAvidinActa crystallographica. Section D, Biological crystallography
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