Search results for "Base Sequence"

showing 10 items of 1146 documents

Isolation of a novel LPS-induced component of the ML superfamily in Ciona intestinalis

2015

ML superfamily represents a group of proteins playing important roles in lipid metabolism and innate immune response. In this study, we report the identification of the first component of the ML superfamily in the invertebrate Ciona intestinalis by means of a subtractive hybridization strategy. Sequence homology and phylogenetic analysis showed that this protein forms a specific clade with vertebrate components of the Niemann-Pick type C2 protein and, for this reason, it has been named Ci-NPC2. The putative Ci-NPC2 is a 150 amino acids long protein with a short signal peptide, seven cysteine residues, three putative lipid binding site and a three-dimensional model showing a characteristic b…

Signal peptideLipopolysaccharidesHemocytesImmunologyMolecular Sequence DataSettore BIO/05 - ZoologiaSequence alignmentBiologyBioinformaticshemic and lymphatic diseasesGene expressionAnimalsCiona intestinalisAmino Acid SequencePeptide sequenceGenePhylogenychemistry.chemical_classificationBase SequenceSequence Homology Amino Acidnutritional and metabolic diseasesbiology.organism_classificationLipid MetabolismImmunity InnateAmino acidCiona intestinalisBiochemistrychemistryLPS NPC2 Ciona intestinalisSuppression subtractive hybridizationCarrier ProteinsSequence AlignmentDevelopmental Biology
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Identification and characterization of onchoastacin, an astacin-like metalloproteinase from the filaria Onchocerca volvulus

2007

Abstract The tissue-invasive nematode Onchocerca volvulus causes skin and eye pathology in human onchocerciasis. While the adult females reside sessile in subcutaneous nodules, the microfilariae are abundantly released from the nodules, males and juvenile worms migrate through the host tissue. Matrix-degrading metallo- and serine proteinases have been detected in excretory-secretory worm products that may be essential for migration of the mobile stages. In this study, a 1713 bp long cDNA encoding for a putative proteinase of O. volvulus has been isolated. The predicted protein sequence includes a signal peptide indicating secretion to the extracellular space, a propeptide, an astacin-like p…

Signal peptideMetalloproteinaseBase SequencebiologyMolecular Sequence DataImmunologyMetalloendopeptidasesOnchocerciasisbiology.organism_classificationMicrobiologyOnchocerca volvulusMicrobiologyOnchocerca volvulusInfectious DiseasesAncylostomaBiochemistryComplementary DNAparasitic diseasesAnimalsHumansAmino Acid SequenceOnchocercaAstacinProtein precursorPhylogenyMicrobes and Infection
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Characterization of two new cuticular genes specifically expressed during the post-ecdysial molting period in Tenebrio molitor

1998

Abstract In a previous study, we have isolated a cDNA, TM-ACP17 , coding for a post-ecdysial adult protein of Tenebrio molitor . After screening of a genomic library with TM-ACP17 , we report isolation and sequencing of TM-ACP17 gene and a new gene, TM-LPCP29 , coding for a larval–pupal protein. These two genes exhibit a common sequence of 15 nucleotides and a characteristic of most cuticular protein genes so far described: an intron interrupting the signal peptide. The deduced aa sequence of TM-LPCP29 exhibits a high percentage of Ala (26.5%) and Val (17.5%) and is highly hydrophobic. In the N-terminal part, the motif VAAPV is repeated ten times. Numerous histidine residues are present in …

Signal peptideMolecular Sequence DataGene ExpressionGenes InsectMoltingBiologyComplementary DNAGeneticsAnimalsGenomic libraryAmino Acid SequenceRNA MessengerTenebrioGeneHistidineMessenger RNAGenomeBase SequenceSequence Homology Amino AcidPupaIntronGene Expression Regulation DevelopmentalDNASequence Analysis DNAGeneral MedicineMolecular biologyGenesBiochemistryLarvaInsect ProteinsMoultingGene
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Candida albicans TDH3 gene promotes secretion of internal invertase when expressed in Saccharomyces cerevisiae as a glyceraldehyde-3-phosphate dehydr…

2003

We have checked the ability of the Candida albicans GAPDH polypeptide, which lacks a conventional N-terminal signal peptide, to reach the cell wall in Saccharomyces cerevisiae by using an intracellular form of the yeast invertase as a reporter protein. A hybrid TDH3-SUC2 gene containing the C. albicans TDH3 promoter sequences and a coding region encoding a fusion protein formed by the C. albicans GAPDH polypeptide, fused at its C-terminus with the yeast internal invertase, was constructed in a centromer derivative plasmid and transformed into a Suc(-) S. cerevisiae strain. Transformants displayed invertase activity measured in intact whole cells, and were able to grow on sucrose as the sole…

Signal peptideSaccharomyces cerevisiae ProteinsGlycoside HydrolasesSaccharomyces cerevisiaeMolecular Sequence DataBioengineeringSaccharomyces cerevisiaeBiologyApplied Microbiology and BiotechnologyBiochemistryGene productFungal ProteinsTransformation Geneticstomatognathic systemCell WallGene Expression Regulation FungalCandida albicansGeneticsAmino Acid SequenceCandida albicansDNA FungalPeptide sequenceGlyceraldehyde 3-phosphate dehydrogenaseBase Sequencebeta-FructofuranosidaseMembrane ProteinsRNA Fungalbiology.organism_classificationBlotting NorthernMolecular biologyFusion proteinRecombinant ProteinsInvertaseBiochemistrybiology.proteinGlyceraldehyde-3-Phosphate Dehydrogenase (Phosphorylating)BiotechnologyPlasmidsYeast (Chichester, England)
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Characterization of a glycosylphosphatidylinositol-bound cell-wall protein (GPI-CWP) in Yarrowia lipolytica.

2004

The structure and composition of the cell wall of yeast has so far been studied mainly in Saccharomyces cerevisiae. It is basically made up of three components: beta-glucans, chitin and mannose-containing glycoproteins, also called mannoproteins. Most covalently bound cell-wall mannoproteins belong to the so-called glycosylphosphatidylinositol cell-wall protein (GPI-CWP) family, cell-wall proteins that are bound through the remnant of a GPI residue to 1,6-beta-glucan. The non-conventional yeast Yarrowia lipolytica shares Generally Regarded As Safe (GRAS) status with S. cerevisiae, has some industrial applications and is increasingly being proposed as a host for the production of recombinant…

Signal peptideSaccharomyces cerevisiae ProteinsGlycosylphosphatidylinositolsSaccharomyces cerevisiaeGenes FungalMolecular Sequence DataYarrowiaSaccharomyces cerevisiaeBiologyMicrobiologyGene productFungal ProteinsSpecies SpecificityCell WallAmino Acid SequenceDNA FungalPeptide sequencechemistry.chemical_classificationMembrane GlycoproteinsBase SequenceSequence Homology Amino AcidFungal geneticsMembrane ProteinsYarrowiabiology.organism_classificationYeastcarbohydrates (lipids)BiochemistrychemistryGlycoproteinMicrobiology (Reading, England)
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Identification and study of a Candida albicans protein homologous to Saccharomyces cerevisiae Ssr1p, an internal cell-wall protein

2003

After screening of aCandida albicansgenome database, the product of an ORF (IPF 3054) that has 62 % homology withSaccharomyces cerevisiaeSsr1p, an internal cell-wall protein, was identified and named CaSsr1p. The deduced amino acid sequence shows that CaSsr1p contains an N-terminal hydrophobic signal peptide, is rich in Ser and Thr amino acids and has a potential glycosylphosphatidylinositol-attachment signal. CaSsr1p is released following degradation of isolated cell walls by zymolyase (mainly a 1,3-β-glucanase) and therefore seems to be covalently linked to theβ-glucan of the cell walls. Both disruption and overexpression of theCaSSR1gene caused an increased sensitivity to calcofluor whit…

Signal peptideSaccharomyces cerevisiae ProteinsMolecular Sequence DataSaccharomyces cerevisiaeGene ExpressionSaccharomyces cerevisiaeCalcofluor-whiteMicrobiologyFungal ProteinsCell wallSpecies SpecificityCell WallCandida albicansAmino Acid SequenceCloning MolecularDNA FungalCandida albicansGenePeptide sequencechemistry.chemical_classificationBase SequenceSequence Homology Amino Acidbiologybiology.organism_classificationAmino acidBiochemistrychemistryGene DeletionMicrobiology
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Sequence of the new Drosophila melanogaster small heat-shock-related gene, lethal(2) essential for life [l(2)efl], at locus 59F4,5.

1995

Abstract In this study, we report the molecular cloning of a novel Drosophila melanogaster small heat-shock (HS)-homologous gene, l(2)efl, identified on the right arm of the second chromosome at locus 59F4,5. We describe the temporal expression of l(2)efl in the wild-type and present its structure. The deduced amino-acid sequence of the Efl protein shows significant homology to all known small HS proteins identified in Drosophila and vertebrates, and to mammalian α-crystallin.

Signal peptideTranscription GeneticMolecular Sequence DataRestriction MappingLocus (genetics)Genes InsectMolecular cloningHomology (biology)biology.animalSequence Homology Nucleic AcidGeneticsAnimalsDrosophila ProteinsAmino Acid SequenceRNA MessengerRelated geneCloning MolecularGeneHeat-Shock ProteinsIn Situ HybridizationGeneticsbiologyBase SequenceSequence Homology Amino AcidVertebrateGeneral MedicineSequence Analysis DNAbiology.organism_classificationDrosophila melanogasterInsect HormonesGenes LethalDrosophila melanogasterGene
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F17-like fimbriae from an invasive Escherichia coli strain producing cytotoxic necrotizing factor type 2 toxin

1994

The F17b fimbriae encoded by the transmissible virulence plasmid Vir, also coding for cytotoxic necrotizing factor type 2, were characterized. A 5.7-kb region of Vir mediates in vitro N-acetylglucosamine-sensitive adhesion to calf intestinal villi. Sequence analysis revealed that this region codes for a structural subunit and an adhesin closely related to the F17-A and F17-G proteins encoded by the F17 fimbrial gene cluster. The F17b-A gene presents an open reading frame of 540 bp encoding a polypeptide of 180 amino acids with a putative signal peptide of 21 residues. The mature protein shows an identity of 74% with the F17-A structural subunit. This 20-kDa protein is recognized by antiseru…

Signal peptideVirulence Factors[SDV]Life Sciences [q-bio]Bacterial ToxinsMolecular Sequence DataImmunologyFimbriaMutantBiologymedicine.disease_causeMicrobiologyMicrobiologyBacterial ProteinsGene clusterEscherichia colimedicineAmino Acid SequenceEscherichia coliPeptide sequenceAdhesins Escherichia coliAntigens BacterialBase SequenceCytotoxinsEscherichia coli ProteinsSEQUENCE NULECOTIDIQUEbiochemical phenomena metabolism and nutritionMolecular biology[SDV] Life Sciences [q-bio]Bacterial adhesinOpen reading frameInfectious DiseasesFimbriae BacterialCLONAGE DE GENEParasitologyResearch ArticleBacterial Outer Membrane ProteinsPlasmidsInfection and Immunity
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Characterization of a cDNA clone encoding a glycine-rich cuticular protein of Tenebrio molitor: developmental expression and effect of a juvenile hor…

1992

0962-1075 (Print) Journal Article; The complete sequence of a cDNA clone, isolated from epidermal mRNA of Tenebrio molitor using a monoclonal antibody raised against an adult-specific cuticular antigen only present in the hard cuticle, was obtained after primer extension at the 5' end. From this cDNA sequence, the deduced protein encompasses 199 amino acids (including a signal peptide) with a total molecular weight of 20.7 kDa. The protein exhibits a bipartite structure: glycine-rich region located in its NH2-terminal part and a carboxy-terminal domain sharing homologies with other cuticular proteins of Orthoptera, Diptera and Lepidoptera. In-situ hybridization analysis shows that the corre…

Signal peptideanimal structuresMethoprene/*pharmacologyCuticleMolecular Sequence DataGlycineBiologyPrimer extensionBiological/drug effects/geneticsComplete sequenceComplementary DNAGeneticsAnimalsAmino Acid SequenceCloning MolecularTenebrioTenebrio/drug effects/*genetics/growth & developmentMolecular BiologyEpidermis/chemistry/growth & developmentProteins/drug effects/*genetics/isolation & purificationchemistry.chemical_classificationMessenger RNABase SequenceMetamorphosisfungiMetamorphosis BiologicalProteinsMolecularSequence Analysis DNADNAMethopreneMolecular biologyAmino acidGlycine/*genetics/metabolismchemistryInsect ScienceJuvenile hormoneInsect ProteinsEpidermisSequence AnalysisCloning
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Systematic screening for mutations in the human serotonin-2A (5-HT2A) receptor gene: Identification of two naturally occurring receptor variants and …

1996

A statistically significant association between a silent mutation (102T/C) in the serotonin-2A (5-HT2A) receptor gene and schizophrenia has recently been reported in a sample of Japanese patients and healthy controls. This finding suggests that genetic predisposition to schizophrenia may be affected by a functional 5-HT2A receptor variant that is in linkage disequilibrium with 102T/C. In the present study, we have sought to identify genetic variation in the 5-HT2A receptor gene by screening genomic DNA samples from 91 unrelated subjects comprising 45 patients with schizophrenia and 46 healthy controls by using single-strand conformation analysis. We have identified four nucleotide sequence …

Silent mutationLinkage disequilibriumMolecular Sequence DataRestriction MappingBiologymedicine.disease_causePolymerase Chain ReactionReference ValuesGenetic variationConfidence IntervalsGeneticsGenetic predispositionmedicineHumansPoint MutationReceptor Serotonin 5-HT2AAmino Acid SequenceAlleleAllele frequencyAllelesGenetics (clinical)DNA PrimersGenetic associationGeneticsMutationPolymorphism GeneticBase SequenceChromosomes Human Pair 13Chromosome MappingGenetic VariationExonsReceptors SerotoninSchizophreniaHuman Genetics
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