Search results for "sequence data"

showing 10 items of 1952 documents

Unexpected associated microalgal diversity in the lichen Ramalina farinacea is uncovered by pyrosequencing analyses

2017

The current literature reveals that the intrathalline coexistence of multiple microalgal taxa in lichens is more common than previously thought, and additional complexity is supported by the coexistence of bacteria and basidiomycete yeasts in lichen thalli. This replaces the old paradigm that lichen symbiosis occurs between a fungus and a single photobiont. The lichen Ramalina farinacea has proven to be a suitable model to study the multiplicity of microalgae in lichen thalli due to the constant coexistence of Trebouxia sp. TR9 and T. jamesii in long-distance populations. To date, studies involving phycobiont diversity within entire thalli are based on Sanger sequencing, but this method see…

0301 basic medicinelcsh:MedicineLichenologyArtificial Gene Amplification and ExtensionPlant SciencePolymerase Chain ReactionDatabase and Informatics MethodsDiversity indexMicroalgaeCluster AnalysisDNA Fungallcsh:ScienceLichenPhylogenyData ManagementMultidisciplinaryEcologybiologyEcologyPhylogenetic AnalysisBiodiversitysymbiosisThallusPhylogeneticspyrosequencingLichenologyTrebouxiaSequence AnalysisResearch ArticleTrebouxiaComputer and Information SciencesBioinformaticsSequence DatabasesReal-Time Polymerase Chain ReactionResearch and Analysis MethodslichenRamalina farinacea03 medical and health sciencesAscomycotaAlgaelichen photobionts pyrosequencing symbiosis TrebouxiaBotanyEvolutionary SystematicsMolecular Biology TechniquesMolecular BiologyDNA sequence analysisTaxonomyEvolutionary BiologyEcology and Environmental Scienceslcsh:RGenetic VariationBiology and Life SciencesSequence Analysis DNAReverse Transcriptase-Polymerase Chain Reactionbiology.organism_classificationBiological Databases030104 developmental biologyphotobiontsPyrosequencinglcsh:QSequence AlignmentPLOS ONE
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Direct Observation of Nanometer-Scale Pores of Melittin in Supported Lipid Monolayers

2015

Melittin is the most studied membrane-active peptide and archetype within a large and diverse group of pore formers. However, the molecular characteristics of melittin pores remain largely unknown. Herein, we show by atomic force microscopy (AFM) that lipid monolayers in the presence of melittin are decorated with numerous regularly shaped circular pores that can be distinguished from nonspecific monolayer defects. The specificity of these pores is reinforced through a statistical evaluation of depressions found in Langmuir-Blodgett monolayers in the presence and absence of melittin, which eventually allows characterization of the melittin-induced pores at a quantitative low-resolution leve…

12-DipalmitoylphosphatidylcholineMolecular Sequence DataPeptideMicroscopy Atomic Forcecomplex mixturesMelittinchemistry.chemical_compoundMicroscopyMonolayerPressureElectrochemistryNanotechnologyMoleculeGeneral Materials ScienceAmino Acid SequencePorositySpectroscopychemistry.chemical_classificationChemistryResolution (electron density)technology industry and agricultureSurfaces and InterfacesCondensed Matter PhysicsLipidsMelittenCrystallographylipids (amino acids peptides and proteins)NanometrePorosityLangmuir
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Stereochemical features of the hydrolysis of 9,10-epoxystearic acid catalysed by plant and mammalian epoxide hydrolases

2002

cis-9,10-Epoxystearic acid was used as a tool to probe the active sites of epoxide hydrolases (EHs) of mammalian and plant origin. We have compared the stereochemical features of the hydrolysis of this substrate catalysed by soluble and membrane-bound rat liver EHs, by soluble EH (purified to apparent homogeneity) obtained from maize seedlings or celeriac roots, and by recombinant soybean EH expressed in yeast. Plant EHs were found to differ in their enantioselectivity, i.e. their ability to discriminate between the two enantiomers of 9,10-epoxystearic acid. For example, while the maize enzyme hydrated both enantiomers at the same rate, the EH from soybean exhibited very high enantioselecti…

1303 BiochemistryStereochemistryMolecular Sequence DataDiol10050 Institute of Pharmacology and Toxicology610 Medicine & healthPolymerase Chain ReactionBiochemistrySubstrate Specificity1307 Cell BiologyHydrolysischemistry.chemical_compound1312 Molecular BiologyAnimalsOrganic chemistryMolecular BiologyDNA PrimersEpoxide HydrolasesMammalschemistry.chemical_classificationBase SequencebiologyChemistryHydrolysisFatty acidActive siteStereoisomerismCell BiologyPlantsRecombinant ProteinsRatsKineticsLiverMicrosomal epoxide hydrolaseEpoxide Hydrolasesbiology.protein570 Life sciences; biologyStereoselectivitySoybeansEnantiomerStearic AcidsResearch Article
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Genomic organization and promoter characterization of the gene encoding a putative endoplasmic reticulum chaperone, ERp29

2002

Abstract ERp29 is a soluble protein localized in the endoplasmic reticulum (ER) of eukaryotic cells, which is conserved in all mammalian species. The N-terminal domain of ERp29 displays sequence and structural similarity to the protein disulfide isomerase despite the lack of the characteristic double cysteine motif. Although the exact function of ERp29 is not yet known, it was hypothesized that it may facilitate folding and/or export of secretory proteins in/from the ER. ERp29 is induced by ER stress, i.e. accumulation of unfolded proteins in the ER. To gain an insight into the mechanisms regulating ERp29 expression we have cloned and characterized the rat ERp29 gene and studied in details …

5' Flanking RegionRecombinant Fusion ProteinsMolecular Sequence DataCHO CellsBiologyCell LineMiceCricetinaeSequence Homology Nucleic AcidGene expressionTumor Cells CulturedGeneticsAnimalsHumansRNA MessengerLuciferasesPromoter Regions GeneticProtein disulfide-isomeraseGeneHeat-Shock ProteinsPhylogenyBase SequenceGene Expression ProfilingEndoplasmic reticulumPromoter3T3 CellsDNAExonsSequence Analysis DNAGeneral MedicineMolecular biologyIntronsRatsHousekeeping geneSecretory proteinGenesUnfolded protein responseFemaleTranscription Initiation SiteSequence AlignmentHeLa CellsGene
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Sequence of a sea urchin hsp70 gene and its 5' flanking region.

1990

We report the nucleotide sequence of a 4470-bp fragment derived from a sea urchin genomic clone containing part of a heat-shock protein 70 (Hsp70)-encoding gene. This fragment, named hsp70 gene II, contains 1271 bp of the flanking region and 3299 bp of structural gene sequence interrupted by five introns and encoding the N-terminal 371 amino acids (aa) of the protein. The 5' flanking region contains a putative TATA element, two CCAAT boxes, four heat-shock consensus sequence elements (hse) and one consensus sequence for binding of Sp1. Remarkable homologies were observed for deduced aa sequence and intron-exon organization between hsp70 gene II and rat hsc73 gene.

5' flanking regionMolecular Sequence DataRestriction MappingBiologyExonSequence Homology Nucleic AcidConsensus SequenceGeneticsConsensus sequenceAnimalsAmino Acid SequencePromoter Regions GeneticGenePeptide sequenceHeat-Shock ProteinsGeneticsBase SequenceStructural geneNucleic acid sequenceGeneral MedicineExonsMolecular biologyIntronsGenesRegulatory sequenceSea UrchinsGene
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Erwinia piriflorinigrans sp. nov., a novel pathogen that causes necrosis of pear blossoms

2010

Eight Erwinia strains, isolated from necrotic pear blossoms in València, Spain, were compared with reference strains of Erwinia amylovora and Erwinia pyrifoliae, both of which are pathogenic to species of pear tree, and to other species of the family Enterobacteriaceae using a polyphasic approach. Phenotypic analyses clustered the novel isolates into one phenon, distinct from other species of the genus Erwinia, showing that the novel isolates constituted a homogeneous phenotypic group. Rep-PCR profiles, PCR products obtained with different pairs of primers and plasmid contents determined by restriction analysis showed differences between the novel strains and reference strains of E. amylovo…

AD-HOC-COMMITTEEBACTERIALFIRE BLIGHT PATHOGENErwiniaPolymerase Chain ReactionErwinia pyrifoliaePyrusRNA Ribosomal 16SCluster Analysis[SDV.BDD]Life Sciences [q-bio]/Development BiologyPhylogenyNESTED-PCRBase Composition0303 health sciencesPEARbiologyPhylogenetic treeNucleic Acid Hybridizationfood and beveragesGeneral MedicineEnterobacteriaceaeBacterial Typing TechniquesTHERMAL-DENATURATIONPlasmidsDNA BacterialGenotypeMolecular Sequence DataDNA RibosomalMicrobiologyMicrobiology03 medical and health sciencesBacterial ProteinsPhylogeneticsDEOXYRIBONUCLEIC-ACIDEcology Evolution Behavior and SystematicsPlant Diseases030304 developmental biologyIDENTIFICATIONSEQUENCES030306 microbiologyAMYLOVORASequence Analysis DNADNARibosomal RNAbiochemical phenomena metabolism and nutrition16S ribosomal RNAbiology.organism_classificationMolecular TypingSpainErwiniabacteria
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Constitutive and regulated α-secretase cleavage of Alzheimer’s amyloid precursor protein by a disintegrin metalloprotease

1999

Amyloid β peptide (Aβ), the principal proteinaceous component of amyloid plaques in brains of Alzheimer’s disease patients, is derived by proteolytic cleavage of the amyloid precursor protein (APP). Proteolytic cleavage of APP by a putative α-secretase within the Aβ sequence precludes the formation of the amyloidogenic peptides and leads to the release of soluble APPsα into the medium. By overexpression ofa disintegrinandmetalloprotease (ADAM), classified as ADAM 10, in HEK 293 cells, basal and protein kinase C-stimulated α-secretase activity was increased severalfold. The proteolytically activated form of ADAM 10 was localized by cell surface biotinylation in the plasma membrane, but the m…

ADAM10Molecular Sequence DataBiologyKidneyTransfectionCell LineSubstrate SpecificityADAM10 ProteinAmyloid beta-Protein PrecursorEndopeptidasesAmyloid precursor proteinAnimalsAspartic Acid EndopeptidasesHumansPoint MutationADAM17 ProteinAmino Acid SequenceCloning MolecularProtein kinase AProtein Kinase CSecretory pathwayBinding SitesMultidisciplinaryHEK 293 cellsP3 peptideMembrane ProteinsMetalloendopeptidasesBiological SciencesPeptide FragmentsRecombinant Proteinscarbohydrates (lipids)ADAM ProteinsKineticsZincAlpha secretaseBiochemistryMutagenesis Site-Directedbiology.proteinCattleAmyloid Precursor Protein SecretasesProceedings of the National Academy of Sciences
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Inducible ASABF-Type Antimicrobial Peptide from the Sponge Suberites domuncula: Microbicidal and Hemolytic Activity in Vitro and Toxic Effect on Moll…

2011

Since sponges, as typical filter-feeders, are exposed to a high load of attacking prokaryotic and eukaryotic organisms, they are armed with a wide arsenal of antimicrobial/cytostatic low-molecular-weight, non-proteinaceous bioactive compounds. Here we present the first sponge agent belonging to the group of ASABF-type antimicrobial peptides. The ASABF gene was identified and cloned from the demospongeSuberites domuncula. The mature peptide, with a length of 64 aa residues has a predicted pI of 9.24, and comprises the characteristic CSαβ structural motif. Consequently, the S. domuncula ASABF shares high similarity with the nematode ASABFs ; it is distantly related to the defensins. The recom…

ASABFAntimicrobial peptidesGastropodaMolecular Sequence DataPharmaceutical SciencePeptideMicrobial Sensitivity TestsGram-Positive BacteriaReal-Time Polymerase Chain ReactionArticleMicrobiology03 medical and health sciencesantimicrobial peptidesAnti-Infective AgentsSequence Analysis ProteinDrug DiscoveryAnimalsBittium sp.Structural motiflcsh:QH301-705.5Pharmacology Toxicology and Pharmaceutics (miscellaneous)spongesPhylogeny030304 developmental biologychemistry.chemical_classification0303 health sciencesbiology030306 microbiologyEffectorHemolytic AgentsapoptosisGeologyBittium spsponges; <em>Suberites domuncula</em>; ASABF; antimicrobial peptides; apoptosis; <em>Bittium</em> sp.biology.organism_classificationSuberites domunculasponges ; Suberites domuncula ; ASABF ; antimicrobial peptides ; apoptosis ; Bittium sp.Recombinant ProteinsSuberites domunculaSpongeEnzymelcsh:Biology (General)chemistryMolluscaSuberitesSuberitesAntimicrobial Cationic PeptidesMarine Drugs
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Genetic organization of the citCDEF locus and identification of mae and clyR genes from Leuconostoc mesenteroides.

1999

ABSTRACT In this paper, we describe two open reading frames coding for a NAD-dependent malic enzyme ( mae ) and a putative regulatory protein ( clyR ) found in the upstream region of citCDEFG of Leuconostoc mesenteroides subsp. cremoris 195. The transcriptional analysis of the citrate lyase locus revealed one polycistronic mRNA covering the mae and citCDEF genes. This transcript was detected only on RNA prepared from cells grown in the presence of citrate. Primer extension experiments suggest that clyR and the citrate lyase operon are expressed from a bidirectional A-T-rich promoter region located between mae and clyR.

ATP citrate lyaseTranscription GeneticOperonMolecular Sequence DataMalatesLocus (genetics)Genetics and Molecular BiologyBiologyMicrobiologyPrimer extensionCitric AcidOpen Reading FramesBacterial ProteinsMalate DehydrogenaseMultienzyme ComplexesLeuconostocAmino Acid SequenceMolecular BiologyGeneGeneticsBase SequenceOxo-Acid-LyasesPromoterGene Expression Regulation BacterialSequence Analysis DNAbiology.organism_classificationMolecular biologyLeuconostoc mesenteroidesGenes BacterialSequence AlignmentLeuconostocJournal of bacteriology
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The Arabidopsis heavy metal P-type ATPase HMA5 interacts with metallochaperones and functions in copper detoxification of roots

2005

*† ‡ § Summary Since copper (Cu) is essential in key physiological oxidation reactions, organisms have developed strategies for handling Cu while avoiding its potentially toxic effects. Among the tools that have evolved to cope with Cu is a network of Cu homeostasis factors such as Cu-transporting P-type ATPases that play a key role in transmembrane Cu transport. In this work we present the functional characterization of an Arabidopsis Cutransporting P-type ATPase, denoted heavy metal ATPase 5 (HMA5), and its interaction with Arabidopsis metallochaperones. HMA5 is primarily expressed in roots, and is strongly and specifically induced by Cu in whole plants. We have identified and characteriz…

ATPaseMolecular Sequence DataMutantArabidopsisPlant ScienceGenes PlantPlant RootsMetallochaperonesArabidopsisGeneticsAmino Acid SequenceRNA MessengerDNA PrimersAdenosine TriphosphatasesBase SequenceSequence Homology Amino AcidbiologyArabidopsis ProteinsCell BiologyCompartmentalization (fire protection)biology.organism_classificationTransmembrane proteinCell biologyBiochemistryChaperone (protein)biology.proteinP-type ATPaseCopperMolecular ChaperonesThe Plant Journal
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