Search results for "Amino acid sequence"

showing 10 items of 1296 documents

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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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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In vivo detection, RNA-binding properties and characterization of the RNA-binding domain of the p7 putative movement protein from carnation mottle ca…

1999

Biochemical and structural characterization studies on the p7 putative movement protein from a Spanish isolate of carnation mottle carmovirus (CarMV) have been conducted. The CarMV p7 gene was fused to a sequence coding for a six-histidine tag and expressed in bacteria, allowing the purification of CarMV p7 and the production of a specific antiserum. This antiserum led to the immunological identification of CarMV p7 in infected leaf tissue from the experimental host Chenopodium quinoa. Putative nucleic acid-binding properties of the CarMV p7 have been explored and demonstrated with both electrophoretic mobility shift and RNA-protein blot in vitro assays using digoxigenin-labeled riboprobes.…

Binding SitesCarmovirusRecombinant Fusion ProteinsMolecular Sequence DataCooperative bindingRNARNA-Binding ProteinsBiologybiology.organism_classificationMolecular biologyPlant Viral Movement ProteinsViral ProteinsBiochemistryVirologyNucleic acidEscherichia coliCarmovirusAmino Acid SequenceMovement proteinPeptide sequenceGeneBinding domainVirology
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Isolation of the Endothelin B Receptor from Bovine Lung Structure, Signal Sequence, and Binding Site

1995

Bovine lung endothelin-B receptor has been isolated in good yield with a new procedure involving the use of endothelin-1 coupled to iminobiotin with a long spacer and avidin-agarose affinity chromatography. Contrary to previous reports, evidence has been obtained that the native form of this receptor corresponds to the full-length transcript expected on the basis of cDNA clones. The binding of endothelin to a variety of shortened fragments of the full receptor suggests that the long N-terminal sequence of this receptor has very little influence on the binding of endothelin and that the main determinants of the endothelin binding site might be constituted by residues in the sixth, and possib…

Binding SitesDNA ComplementaryEndothelin receptor type AReceptors EndothelinEndothelinsMolecular Sequence DataBiologyReceptor Endothelin BBiochemistryEndothelin 1Molecular biologyChromatography AffinityBiochemistrycardiovascular systemEnzyme-linked receptorAnimalsCattleElectrophoresis Polyacrylamide Gel5-HT5A receptorAmino Acid SequenceBinding siteGABBR1Endothelin receptorLungProtease-activated receptor 2European Journal of Biochemistry
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Self-assembly of bioelastomeric structures from solutions: Mean-field critical behavior and Flory-Huggins free energy of interactions

1993

Elastic and quasi-elastic light scattering studies were performed on aqueous solutions of poly (Val-Pro-Gly-Gly), a representative synthetic bioelastomer that differs from the previously studied poly (Val-Pro-Gly-Val-Gly) by the deletion of the hydrophobic Val in position four. When the spinodal line was approached from the region of thermodynamic stability, the intensity of light scattered by fluctuations, and the related lifetime and correlation length, were observed to diverge with mean-field critical exponents for both systems. Fitting of the experimental data allowed determining the spinodal and binodal (coexistence) lines that characterize the phase diagrams of the two systems, and it…

BinodalSpinodalProtein ConformationChemistryMolecular Sequence DataOrganic ChemistryBiophysicsSortingThermodynamicsGeneral MedicineStatistical fluctuationsFlory–Huggins solution theoryBiochemistryLight scatteringSolutionsBiomaterialsMean field theoryThermodynamicsPhysical chemistryAmino Acid SequenceRubberPeptidesCritical exponentBiopolymers
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Phosphorylation of serine residues is fundamental for the calcium-binding ability of Orchestin, a soluble matrix protein from crustacean calcium stor…

2003

International audience; Orchestia cavimana is a terrestrial crustacean, which cyclically stores calcium in diverticula of the midgut, in the form of calcified amorphous concretions. These concretions are associated with a proteinaceous matrix, the main constituent of the soluble matrix is Orchestin, an acidic calcium-binding protein [Testenière et al., Biochem. J. 361 (2002) 327-335]. In the present paper, we clearly demonstrate that Orchestin is phosphorylated on serine and tyrosine residues, but that calcium binding only occurs via the phosphoserine residues. To our knowledge, this is the first example of an invertebrate mineralization for which a post-translational modification is clearl…

BiomineralizationMESH: Amino Acid SequenceMESH: Calcium-Binding ProteinsMatrix (biology)01 natural sciencesBiochemistryCalcium in biologyMESH: TyrosineSerinechemistry.chemical_compoundMESH: Structure-Activity RelationshipStructural BiologyCrustaceaSerineElectrophoresis Gel Two-DimensionalMESH: AnimalsTyrosinePhosphorylation0303 health sciencesBiochemistryMESH: CalciumPhosphorylationElectrophoresis Polyacrylamide GelOrganic matrixProtein BindingMolecular Sequence DataBiophysicschemistry.chemical_elementCrustaceanCalciumBiology010402 general chemistryMESH: Calcification Physiologic03 medical and health sciencesStructure-Activity RelationshipCalcification PhysiologicMESH: CrustaceaGeneticsAnimalsMESH: Protein Binding[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid SequenceMESH: SerineMolecular Biology030304 developmental biologyCalcium metabolismMESH: Molecular Sequence DataMESH: PhosphorylationCalcium-Binding ProteinsCell BiologyMESH: Electrophoresis Gel Two-Dimensional0104 chemical scienceschemistryPhosphoserineMESH: Protein Processing Post-TranslationalTyrosineCalciumCalcium bindingProtein Processing Post-TranslationalMESH: Electrophoresis Polyacrylamide Gel
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Insertion and Topology of a Plant Viral Movement Protein in the Endoplasmic Reticulum Membrane

2002

Virus-encoded movement proteins (MPs) mediate cell-to-cell spread of viral RNA through plant membranous intercellular connections, the plasmodesmata. The molecular pathway by which MPs interact with viral genomes and target plasmodesmata channels is largely unknown. The 9-kDa MP from carnation mottle carmovirus (CarMV) contains two potential transmembrane domains. To explore the possibility that this protein is in fact an intrinsic membrane protein, we have investigated its insertion into the endoplasmic reticulum membrane. By using in vitro translation in the presence of dog pancreas microsomes, we demonstrate that CarMV p9 inserts into the endoplasmic reticulum without the aid of any addi…

BioquímicaGlycosylationMolecular Sequence DataPlasmodesmaBiologyEndoplasmic ReticulumTopologyBiochemistryProtein Structure SecondaryViral ProteinsAmino Acid SequenceMolecular BiologyEndoplasmic reticulumCarmovirusProteïnes de membranaMembrane ProteinsSTIM1Translation (biology)Cell Biologybiology.organism_classificationVirusCell biologyPlant Viral Movement ProteinsTobacco Mosaic VirusTransmembrane domainCytoplasmMembrane topologyCarmovirusJournal of Biological Chemistry
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Production and characterisation of recombinant forms of human pulmonary surfactant protein C (SP-C):Structure and surface activity

2006

  Udgivelsesdato: 2006-Apr Surfactant protein C (SP-C) is an essential component for the surface tension-lowering activity of the pulmonary surfactant system. It contains a valine-rich alpha helix that spans the lipid bilayer, and is one of the most hydrophobic proteins known so far. SP-C is also an essential component of various surfactant preparations of animal origin currently used to treat neonatal respiratory distress syndrome (NRDS) in preterm infants. The limited supply of this material and the risk of transmission of infectious agents and immunological reactions have prompted the development of synthetic SP-C-derived peptides or recombinant humanized SP-C for inclusion in new prepar…

BioquímicaRecombinant membrain proteinSurface PropertiesSize-exclusion chromatographyMolecular Sequence DataPhospholipidBiophysicsBiologyBiochemistrylaw.inventionchemistry.chemical_compoundAffinity chromatographyPulmonary surfactantMembranes (Biologia)lawAnimalsHumansPulmonary surfactant-associated protein CAmino Acid SequenceLipid bilayerConserved SequencePhospholipidsMammalsDrug CarriersChromatographySequence Homology Amino AcidSP-CProteïnes de membranaSurfactant protein CPulmonary surfactantCell BiologyPulmonary Surfactant-Associated Protein CRecombinant ProteinsKineticschemistryBiochemistryRecombinant DNALipid-protein interactionPeptidesSequence Alignment
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Ionic self-complementarity induces amyloid-like fibril formation in an isolated domain of a plant copper metallochaperone protein

2004

This article is available from: http://www.biomedcentral.com/1472-6807/4/7

BioquímicaSerum Amyloid A Proteinendocrine systemArabidopsis ProteinsProtein ConformationMolecular Sequence DataOsmolar ConcentrationArabidopsisBiological TransportProtein Structure Secondarylcsh:Biology (General)Amino Acid SequencePeptidesProteïneslcsh:QH301-705.5CopperMolecular ChaperonesResearch Article
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Specific expression of a TRIM-containing factor in ectoderm cells affects the skeletal morphogenetic program of the sea urchin embryo

2011

In the indirect developing sea urchin embryo, the primary mesenchyme cells (PMCs) acquire most of the positional and temporal information from the overlying ectoderm for skeletal initiation and growth. In this study, we characterize the function of the novel gene strim1, which encodes a tripartite motif-containing (TRIM) protein, that adds to the list of genes constituting the epithelial-mesenchymal signaling network. We report that strim1 is expressed in ectoderm regions adjacent to the bilateral clusters of PMCs and that its misexpression leads to severe skeletal abnormalities. Reciprocally, knock down of strim1 function abrogates PMC positioning and blocks skeletogenesis. Blastomere tran…

BlastomeresDNA Complementaryanimal structuresTRIM Sea urchin embryo Ectoderm Skeleton biomineralization Morpholino oligonucleotides Primary mesenchyme Cell migration Guidance otp pax2/5/8 sm30MesenchymeMolecular Sequence DataMorphogenesisSettore BIO/11 - Biologia MolecolareEctodermBiologyLigandsModels BiologicalBone and BonesMesodermCell MovementEctodermGene expressionmedicineAnimalsAmino Acid SequenceMolecular BiologyGeneGeneticsBone DevelopmentSequence Homology Amino AcidGene Expression Regulation DevelopmentalEmbryoBlastomereProtein Structure TertiaryCell biologyTransplantationmedicine.anatomical_structureSea Urchinsembryonic structuresCarrier ProteinsDevelopmental BiologyDevelopment
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