Search results for "DOMAINS"

showing 10 items of 269 documents

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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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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Cloning and expression of the putative aggregation factor from the marine sponge Geodia cydonium.

2001

Sponges (phylum Porifera) have extensively been used as a model system to study cell-cell interaction on molecular level. Recently, we identified and cloned the putative aggregation receptor (AR) of the sponge Geodia cydonium, which interacts in a heterophilic way with the aggregation factor (AF) complex. In the present study, antibodies against this complex have been raised that abolish the adhesion function of the enriched sponge AF, the AF-Fraction 6B. Using this antibody as a tool, a complete 1.7 kb long cDNA, GEOCYAF, could be isolated from a cDNA library that encodes the putative AF. Its deduced aa sequence in the N-terminal section comprises high similarity to amphiphysin/BIN1 sequen…

DNA ComplementaryBlotting WesternMolecular Sequence DataBiologyModels BiologicalSH3 domainAntibodieslaw.inventionEvolution Molecularsrc Homology DomainslawComplementary DNACell AdhesionEscherichia coliAnimalsAmino Acid SequenceBinding siteCloning MolecularPhylogenyGalectinCell AggregationGene LibraryCloningDose-Response Relationship DrugSequence Homology Amino AcidcDNA libraryCell MembraneCell BiologySequence Analysis DNAMolecular biologyRecombinant ProteinsPoriferaProtein Structure TertiaryAmphiphysinRecombinant DNAPeptidesCell Adhesion MoleculesProtein BindingJournal of cell science
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Src proteins/src genes: from sponges to mammals

2004

The genome of marine sponge Suberites domuncula, a member of the most ancient and most simple metazoan phylum Porifera, encodes at least five genes for Src-type proteins, more than, i.e., Caenorhabditis elegans or Drosophila melanogaster (two in each). Three proteins, SRC1SD, SRC2SD and SRC3SD, were fully characterized. The overall homology (identity+similarity) among the three S. domuncula Srcs (68-71%) is much lower than the sequence conservation between orthologous Src proteins from freshwater sponges (82-85%). It is therefore very likely that several src genes/proteins were already present in the genome of Urmetazoa, the hypothetical metazoan ancestor. We have identified in the S. domun…

DNA Complementaryanimal structuresMolecular Sequence DataProto-Oncogene Proteins pp60(c-src)SH2 domainHomology (biology)SH3 domainEvolution Molecularsrc Homology DomainsExonGeneticsAnimalsProtein IsoformsAmino Acid SequenceCloning MolecularGenePhylogenyMammalsGeneticsSequence Homology Amino AcidbiologyIntronDNASequence Analysis DNAGeneral Medicinebiology.organism_classificationIntronsPoriferaSuberites domunculaSequence AlignmentProto-oncogene tyrosine-protein kinase SrcGene
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Structure of SNX9 SH3 in complex with a viral ligand reveals the molecular basis of its unique specificity for alanine-containing class I SH3 motifs

2021

Class I SH3 domain-binding motifs generally comply with the consensus sequence [R/K]x0PxxP, the hydrophobic residue 0 being proline or leucine. We have studied the unusual 0 = Ala-specificity of SNX9 SH3 by determining its complex structure with a peptide present in eastern equine encephalitis virus (EEEV) nsP3. The structure revealed the length and composition of the n-Src loop as important factors determining specificity. We also compared the affinities of EEEV nsP3 peptide, its mutants, and cellular ligands to SNX9 SH3. These data suggest that nsP3 has evolved to minimize reduction of conformational entropy upon binding, hence acquiring stronger affinity, enabling takeover of SNX9. The R…

DYNAMICSPROLINE-RICH PEPTIDESviruksetPROTEINSvirusesHTLV-1 GagLigandsEVOLUTIONARY CONSERVATIONalfaviruksetsrc Homology DomainsHIGH-AFFINITYretroviruksetDOMAINStructural BiologyBINDINGAnimalsHorsesMolecular Biologysoluviestintä11832 Microbiology and virologyAlanineBinding SitesPXXP MOTIFSisothermal titration calorimetrySH3solution NMR spectroscopyEEEV nsP3HIV-11182 Biochemistry cell and molecular biologyproteiinitCHEMICAL-SHIFTS3111 BiomedicinePeptidesSNX9Protein Binding
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CD95 death-inducing signaling complex formation and internalization occur in lipid rafts of type I and type II cells

2004

We investigated the membrane localization of CD95 in type I and type II cells, which differ in their ability to recruit and activate caspase-8. We found that CD95 was preferentially located in lipid rafts of type I cells, while it was present both in raft and non-raft plasma membrane sub-domains of type II cells. After stimulation, CD95 located in phospholipid-rich plasma membrane was recruited to lipid rafts in both types of cells. Similarly, CD95 cross-linking resulted in caspase-independent translocation of FADD/MORT1 and caspase-8 to the lipid rafts, which was prevented by a death domain-defective receptor. CD95 internalization was then rapid in type I and delayed in type II cells and s…

Death Domain Receptor Signaling Adaptor ProteinsEndosomeT-Lymphocytesmedia_common.quotation_subjectImmunologyApoptosisReceptors Tumor Necrosis FactorCell LineMembrane MicrodomainsSettore MED/04 - PATOLOGIA GENERALECell Line TumorReceptorsHumansImmunology and Allergyfas ReceptorFADDInternalizationLipid raftLipid raftsDeath domainmedia_commonTumorbiologyVesicleFas receptorEndocytosisCell biologyProtein TransportCholesterolCD95 death-inducing signaling complexCaspasesCD95biology.proteinlipids (amino acids peptides and proteins)biological phenomena cell phenomena and immunityCaspase-8Tumor Necrosis FactorCaspase-8; CD95; Lipid rafts; Apoptosis; Caspases; Cell Line Tumor; Cholesterol; Death Domain Receptor Signaling Adaptor Proteins; Humans; Membrane Microdomains; Protein Binding; Protein Transport; Receptors Tumor Necrosis Factor; T-Lymphocytes; fas Receptor; Endocytosis; Signal Transduction; Immunology and Allergy; ImmunologyProtein BindingSignal TransductionEuropean Journal of Immunology
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Characterization of denitrification gene clusters of soil bacteria via a metagenomic approach

2009

International audience; Denitrification is a microbial respiratory process contributing to the emission of greenhouse gas. The study of denitrifying bacteria, like that of others, is hindered by characteristics that can prevent up to 99% of soil bacteria from being cultivated in vitro. New approaches based on the direct extraction of DNA from the natural environment and PCR amplifications can overcome limitations due to bacterial unculturability, but until now their application to denitrification genes has led only to the recovery of partial sequences for some of these genes.Our goals in this study were to apply a metagenomic approach characterized by cloning of DNA extracted from soil and …

Denitrification[SDV]Life Sciences [q-bio]Microbial metabolismNIRKApplied Microbiology and Biotechnology[ SPI.NRJ ] Engineering Sciences [physics]/Electric powerGene OrderGene clusterPHYLOGENETIC ANALYSISNITROUS-OXIDE REDUCTASESoil MicrobiologyComputingMilieux_MISCELLANEOUS2. Zero hunger0303 health sciencesdenitrificationEcologyfood and beveragesFAMILYCOMMUNITYPCRMultigene Family[SDE]Environmental SciencesSoil microbiologyMetabolic Networks and PathwaysBiotechnologyDNA BacterialDOMAINSNitrogenMolecular Sequence DataComputational biologyBiologyMicrobial Ecologysoil03 medical and health sciencesmetagenomic;n-cycle;denitrification;soil Bacterial ProteinsOperonBotanymetagenomicNitrogen cycle030304 developmental biology[ SDE.BE ] Environmental Sciences/Biodiversity and EcologyNITRIC-OXIDEBacteriaSequence Homology Amino Acid030306 microbiology[SPI.NRJ]Engineering Sciences [physics]/Electric powerSequence Analysis DNAn-cyclebiology.organism_classificationDENITRIFYING PSEUDOMONAS-STUTZERIMetagenomicsPyrosequencing[SDE.BE]Environmental Sciences/Biodiversity and EcologyBacteria[SPI.NRJ] Engineering Sciences [physics]/Electric powerFood ScienceNOSZ GENES
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Multiple positive solutions for singularly perturbed elliptic problems in exterior domains

2003

Abstract The equation − e 2 Δ u + a e ( x ) u = u p −1 with boundary Dirichlet zero data is considered in an exterior domain Ω = R N ⧹ ω ( ω bounded and N ⩾2). Under the assumption that a e ⩾ a 0 >0 concentrates round a point of Ω as e →0, that p >2 and p N /( N −2) when N ⩾3, the existence of at least three positive distinct solutions is proved.

Dirichlet problemPure mathematicsPartial differential equationApplied MathematicsMathematical analysisZero (complex analysis)Boundary (topology)Exterior domains; lack of compactness; multiplicity of solutionslack of compactnessDirichlet distributionExterior domainsmultiplicity of solutionssymbols.namesakeBounded functionDomain (ring theory)symbolsMathematical PhysicsAnalysisMathematics
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Dirichlet Forms, Poincaré Inequalities, and the Sobolev Spaces of Korevaar and Schoen

2004

We answer a question of Jost on the validity of Poincare inequalities for metric space-valued functions in a Dirichlet domain. We also investigate the relationship between Dirichlet domains and the Sobolev-type spaces introduced by Korevaar and Schoen.

Discrete mathematicsDirichlet formMathematics::Analysis of PDEsDirichlet L-functionDirichlet's energyMathematics::Spectral Theorysymbols.namesakeDirichlet kernelDirichlet's principlesymbolsGeneral Dirichlet seriesAnalysisDirichlet seriesMathematicsSobolev spaces for planar domainsPotential Analysis
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Sobolev embeddings, extensions and measure density condition

2008

AbstractThere are two main results in the paper. In the first one, Theorem 1, we prove that if the Sobolev embedding theorem holds in Ω, in any of all the possible cases, then Ω satisfies the measure density condition. The second main result, Theorem 5, provides several characterizations of the Wm,p-extension domains for 1<p<∞. As a corollary we prove that the property of being a W1,p-extension domain, 1<p⩽∞, is invariant under bi-Lipschitz mappings, Theorem 8.

Discrete mathematicsExtension operator010102 general mathematicsEberlein–Šmulian theoremMeasure density condition01 natural sciencesSobolev embeddingSobolev inequality010101 applied mathematicsSobolev spaceCorollarySobolev spaces0101 mathematicsInvariant (mathematics)AnalysisEdge-of-the-wedge theoremSobolev spaces for planar domainsMathematicsTrace operatorJournal of Functional Analysis
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