Search results for "Molecular sequence"

showing 10 items of 1972 documents

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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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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Mitochondrial DNA Regionalism and Historical Demography in the Extant Populations of Chirocephalus kerkyrensis (Branchiopoda: Anostraca)

2012

BackgroundMediterranean temporary water bodies are important reservoirs of biodiversity and host a unique assemblage of diapausing aquatic invertebrates. These environments are currently vanishing because of increasing human pressure. Chirocephalus kerkyrensis is a fairy shrimp typical of temporary water bodies in Mediterranean plain forests and has undergone a substantial decline in number of populations in recent years due to habitat loss. We assessed patterns of genetic connectivity and phylogeographic history in the seven extant populations of the species from Albania, Corfu Is. (Greece), Southern and Central Italy.Methodology/principal findingsWe analyzed sequence variation at two mito…

Base Pair MismatchScienceMolecular Sequence DataPopulation DynamicsBiodiversitySettore BIO/05 - ZoologiaPopulation geneticsBranchiopodaMarine and Aquatic SciencesMarine BiologyChirocephalus kerkyrensis Anostraca Phylogeography Mediterranean Temporary PondsExtinction BiologicalDNA MitochondrialHaplogroupGene flowLimnologyAnimalsCluster AnalysisEvolutionary SystematicsBiologyPhylogenyInstitut für Biochemie und BiologieDemographyEvolutionary BiologyMultidisciplinarybiologyEcologyPopulation BiologyEcologyMediterranean RegionQRGenetic VariationPaleontologybiology.organism_classificationPhylogeographyPhylogeographyHabitat destructionHaplotypesAnostracaEarth SciencesMedicineAnostracaZoologyResearch Article
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Direct detection of repetitive, whole chromosome paint and telomere DNA probes by immunogold electron microscopy

1993

Biotinylated repetitive, whole chromosome paint and telomere DNA probes were investigated at the electron microscope level after non-isotopic in situ hybridization and direct immunogold detection. The protocol described allowed the visualization of a biotinylated chromosome 1 specific satellite DNA probe in the light microscope without silver intensification. This sensitive method was exploited to analyse factors contributing to signal strength in immunogold chromosome painting. Furthermore, it allowed us to investigate the distribution of (TTAGGG)n telomere repeats in human metaphase chromosomes and interphase nuclei. Telomeric and internal (TTAGGG)n repeats were detected at high spatial r…

Base SequenceSatellite DNAHybridization probeMolecular Sequence DataChromosomeQ-FISHImmunogold labellingTelomereBiologyMolecular biologyTelomereGeneticsBiophysicsChromosomes HumanHumansInterphaseLymphocytesDNA ProbesMicroscopy ImmunoelectronInterphaseMetaphaseIn Situ HybridizationRepetitive Sequences Nucleic AcidChromosome Research
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Morphological and molecular taxonomy ofPythium longisporangiumsp. nov. isolated from the Burgundian region of France

2005

During the course of an investigation on the Pythiaceous oomycetes occurring in the Burgundian vineyards, some species of Pythium possessing mainly hypogynous antheridia were found. These had been classified as oomycetes belonging to the ‘‘Pythium rostratum’’ group for a long time. Three of these isolates, having similar structures and growth, are very closely related to a recently described species, Pythium bifurcatum Paul. A close look at these, however, underlines some fundamental differences with the latter. Not all of them produce zoospores but have very large sporangia. The type specimen is F-1200 (B 76a) which is a medium-slow growing saprophyte. The sequence of the ITS region of the…

Base SequenceSporangiumMolecular Sequence DataPythiumWineSequence Analysis DNAFungi imperfectiRibosomal RNABiologybiology.organism_classificationPolymerase Chain ReactionMicrobiologyRNA RibosomalAntheridiumDNA Ribosomal SpacerBotanyGeneticsOosporeTaxonomy (biology)FrancePythiumSequence AlignmentMolecular BiologyRibosomal DNASoil MicrobiologyFEMS Microbiology Letters
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Cloning and characterization of the phenylalanyl-tRNA synthetase β subunit gene fromCandida albicans

1998

A Candida albicans expression library was constructed from RNA isolated from regenerating protoplasts. A 1.4-kb cDNA clone was used to isolate a genomic fragment. Sequence analysis revealed an open reading frame of 593 amino acids with an overall identity of 63.6% with the phenylalanyl-tRNA synthetase beta subunit (FRS1) of Saccharomyces cerevisiae. We named it CaFRS1. It is located in a single copy in chromosome R, SfiI fragment M. Its expression showed a decrease during the cell wall regeneration process in protoplasts of both yeast and mycelial cells of C. albicans, suggesting its requirement thereof in initial steps of the cell wall synthesis.

Base SequencebiologyGenes FungalMolecular Sequence DataSaccharomyces cerevisiaeNucleic acid sequenceRNAMolecular cloningbiology.organism_classificationMicrobiologyMolecular biologyCorpus albicansBlotting SouthernOpen reading frameBiochemistryCell WallCandida albicansGeneticsPhenylalanine-tRNA LigaseAmino Acid SequenceCloning MolecularCandida albicansMolecular BiologyGeneFEMS Microbiology Letters
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