Search results for "signal peptide"

showing 10 items of 60 documents

Structures of two molluscan hemocyanin genes: significance for gene evolution.

2001

We present here the description of genes coding for molluscan hemocyanins. Two distantly related mollusks, Haliotis tuberculata and Octopus dofleini , were studied. The typical architecture of a molluscan hemocyanin subunit, which is a string of seven or eight globular functional units (FUs, designated a to h, about 50 kDa each), is reflected by the gene organization: a series of eight structurally related coding regions in Haliotis , corresponding to FU-a to FU-h, with seven highly variable linker introns of 174 to 3,198 bp length (all in phase 1). In Octopus seven coding regions (FU-a to FU-g) are found, separated by phase 1 introns varying in length from 100 bp to 910 bp. Both genes exh…

GeneticsSignal peptideUntranslated regionMultidisciplinarySequence Homology Amino Acidmedicine.medical_treatmentMolecular Sequence DataIntronHemocyaninDNAExonsBiologyBiological SciencesBiological EvolutionIntronsExonSpecies SpecificityMolluscaHemocyaninsmedicineCoding regionAnimalsAmino Acid SequencePeptide sequenceGeneProceedings of the National Academy of Sciences of the United States of America
researchProduct

Ciona intestinalis galectin (CiLgals-a and CiLgals-b) genes are differentially expressed in endostyle zones and challenged by LPS

2015

Abstract Immunohistochemical and in situ hybridization assays were performed to answer the question whether the endostyle, that is the initial gastro-intestinal trait of Ciona intestinalis pharynx, is involved in galectin (CiLgals-a and CiLgals-b) production during the pharynx inflammatory response to LPS inoculation. Specific anti-CiLgal-a and anti-CiLgals-b antibodies, and oligonucleotide probes, that mark inflammatory hemocytes inside the pharynx vessels and vessel epithelium as shown by a previous paper, were assayed on endostyle histological sections. For the first time, we show that galectins are produced by endostyle zones, and both CiLgals-a and –b genes are upregulated by LPS. CiLg…

LipopolysaccharidesSignal peptideLPSAscidianGalectinsOligonucleotidesSettore BIO/05 - ZoologiaIn situ hybridizationAquatic ScienceBiologyendostyleDownregulation and upregulationotorhinolaryngologic diseasesmedicineExtracellularAnimalsEnvironmental ChemistryCiona intestinalisIn Situ HybridizationGalectinAscidian Galectin Endostyle Inflammation Ciona intestinalisgalectinGeneral Medicinebiology.organism_classificationImmunohistochemistryMolecular biologyEpitheliumCiona intestinalismedicine.anatomical_structureItalyinflammationImmunologyPharynxEndostyle
researchProduct

A functional analysis of ACP-20, an adult-specific cuticular protein gene from the beetle Tenebrio. Role of an intronic sequence in transcriptional a…

2004

0962-1075 (Print) Comparative Study Journal Article Research Support, Non-U.S. Gov't; A gene encoding the adult cuticular protein ACP-20 was isolated in Tenebrio. It consists of three exons interspersed by two introns, intron 1 interrupting the signal peptide. To understand the regulatory mechanisms of ACP-20 expression, ACP-20 promoter-luciferase reporter gene constructs were transfected into cultured pharate adult wing epidermis. Transfection assays needed the presence of 20-hydroxyecdysone, confirming that ACP-20 is up-regulated by ecdysteroids. Analysis of 5' deletion constructs revealed that three regions are necessary for high levels of transcription. Interaction experiments between i…

MESH : Molecular Sequence Data[ SDV.AEN ] Life Sciences [q-bio]/Food and NutritionMESH : Genes Reporter/physiologyMESH : Transcriptional Activation/geneticsMESH : Introns/geneticsPromoter Regions (Genetics)/drug effects/physiologyExon0302 clinical medicineGenes ReporterTranscriptional regulationTrans-Activation (Genetics)/genetics/*physiologyMESH : Tenebrio/geneticsLuciferasesPromoter Regions GeneticTenebrioPeptide sequenceMESH : Metamorphosis Biological/geneticsComputingMilieux_MISCELLANEOUS0303 health sciencesMESH : Amino Acid SequenceMetamorphosis BiologicalMESH : Luciferases/metabolismEcdysone/metabolism/pharmacology3. Good healthInsect ProteinsMESH : TransfectionSequence AnalysisSignal peptideTranscriptional ActivationEcdysoneanimal structuresSequence analysisMolecular Sequence DataMESH : Transcriptional Activation/physiologyReporter/physiologyBiological/genetics/*physiologyMESH : Insect Proteins/physiologyBiologyLuciferases/metabolismTransfectionTenebrio/*genetics/physiologyMESH : Ecdysone/pharmacology03 medical and health sciencesGeneticsAnimalsAmino Acid Sequence[ SDV.BDD ] Life Sciences [q-bio]/Development BiologyMolecular BiologyGeneMESH : Introns/physiology030304 developmental biologyGene LibraryMESH : Metamorphosis Biological/physiologyReporter gene[SDV.GEN.GPO]Life Sciences [q-bio]/Genetics/Populations and Evolution [q-bio.PE]Base SequenceMetamorphosisIntronIntrons/genetics/physiologyMESH : Ecdysone/metabolismSequence Analysis DNADNAMESH : Gene LibraryMolecular biologyIntronsGenesMESH : Tenebrio/physiologyEpidermis/metabolism Gene LibraryInsect ScienceMESH : Insect Proteins/geneticsMESH : Epidermis/metabolismMESH : Base SequenceMESH : AnimalsEpidermisMESH : Promoter Regions Genetic/drug effects[SDE.BE]Environmental Sciences/Biodiversity and EcologyInsect Proteins/*genetics/*physiology030217 neurology & neurosurgeryEpidermis/metabolismMESH : Promoter Regions Genetic/physiologyMESH : Sequence Analysis DNA
researchProduct

Evolutionary Dissection of the Dot/Icm System Based on Comparative Genomics of 58 Legionella Species

2019

14 páginas, 2 figuras, 2 tablas

MESH: Selection GeneticLegionella pneumophilaMESH: Bacterial Proteins/metabolism*Negative selectionPositive-selectionDot/Icm systemMESH: PhylogenyNegative-selectionPhylogenyMESH: Evolution MolecularRecombination Genetic0303 health sciencesEffectorMESH: GenomicsGenomics3. Good healthCell biologypositive-selectionDiversifying-selectionMESH: Recombination GeneticMESH: Membrane ProteinsResearch ArticleSignal peptidenegative-selectionEvolutionLegionellaMESH: Carrier ProteinsBiologyMESH: Bacterial Proteins/geneticsEvolution MolecularType IV Secretion Systems03 medical and health sciencesdiversifying-selectionMESH: Type IV Secretion Systems*Bacterial Proteins[SDV.BBM.GTP]Life Sciences [q-bio]/Biochemistry Molecular Biology/Genomics [q-bio.GN]evolutionGeneticsSecretionSelection GeneticEcology Evolution Behavior and SystematicsMESH: Legionella/classification030304 developmental biologyComparative genomicsMESH: Legionella/metabolism030306 microbiologyMESH: Legionella/geneticsMembrane ProteinsPeriplasmic spacebiology.organism_classificationCytoplasmCarrier Proteins
researchProduct

An impaired peroxisomal targeting sequence leading to an unusual bicompartmental distribution of cytosolic epoxide hydrolase

1991

AbstractTo gain an understanding of the mechanism by which the subcellular distribution of cytosolic epoxide hydrolase (cEH) is directed, we have analyzed the carboxy terminal region of rat liver cEH by means of cDNA cloning to define the structure of its possible peroxisomal targeting sequence (PTS). Purified cEH was subjected to peptide analysis following endoproteinase Glu-C digestion and HPLC-separation of the fragments. The obtained sequence information was used to perform PCR experiments resulting in the isolation of a 680 bp cDNA clone encoding the carboxy terminus of cEH. The deduced amino acid sequence displays a terminal tripeptide Ser-Lys-Ile which is highly homologous to the PTS…

MaleSignal peptidePTSanimal structures1303 BiochemistryMolecular Sequence DataBiophysics10050 Institute of Pharmacology and Toxicology610 Medicine & healthTripeptideProtein Sorting SignalsBiologyMicrobodiesBiochemistryAmino acid sequence1307 Cell BiologyCytosol1315 Structural Biology1311 GeneticsStructural BiologyComplementary DNAGenetics1312 Molecular BiologyAnimalsCloning MolecularEpoxide hydrolaseMolecular BiologyPeptide sequenceEpoxide Hydrolaseschemistry.chemical_classificationBase SequencecDNA sequenceDNACell BiologyPeroxisomeMolecular biologyRatsIsoenzymesCytosolPCREnzymeLiverchemistryBiochemistrycEH570 Life sciences; biologyPeptide analysis1304 Biophysics
researchProduct

Functional and structural insights into astacin metallopeptidases

2012

The astacins are a family of multi-domain metallopeptidases with manifold functions in metabolism. They are either secreted or membrane-anchored and are regulated by being synthesized as inactive zymogens and also by colocalizing protein inhibitors. The distinct family members consist of N-terminal signal peptides and pro-segments, zincdependent catalytic domains, further downstream extracellular domains, transmembrane anchors, and cytosolic domains. The catalytic domains of four astacins and the zymogen of one of these have been structurally characterized and shown to comprise compact ~200-residue zinc-dependent moieties divided into an N-terminal and a C-terminal sub-domain by an active-s…

MetzincinSignal peptideStereochemistryMolecular Sequence DataClinical BiochemistryTolloidMatrix metalloproteinaseBiologyBiochemistryEvolution Molecular03 medical and health sciencesEnzyme activatorBone morphogenetic proteinsZymogenAnimalsHumansProtease InhibitorsAmino Acid SequenceTyrosineMolecular BiologyPeptide sequence030304 developmental biologyEnzyme Precursors0303 health sciences030302 biochemistry & molecular biologyMetalloendopeptidasesMeprinTransmembrane protein3. Good healthEnzyme ActivationBiochemistryAstacinCatalytic domainsbchm
researchProduct

The Sequence of a Gastropod Hemocyanin (HtH1 from Haliotis tuberculata)

2000

The eight functional units (FUs), a-h, of the hemocyanin isoform HtH1 from Haliotis tuberculata (Prosobranchia, Archaeogastropoda) have been sequenced via cDNA, which provides the first complete primary structure of a gastropod hemocyanin subunit. With 3404 amino acids (392 kDa) it is the largest polypeptide sequence ever obtained for a respiratory protein. The cDNA comprises 10,758 base pairs and includes the coding regions for a short signal peptide, the eight different functional units, a 3'-untranslated region of 478 base pairs, and a poly(A) tail. The predicted protein contains 13 potential sites for N-linked carbohydrates (one for HtH1-a, none for HtH1-c, and two each for the other si…

Models MolecularSignal peptideDNA ComplementaryProtein subunitmedicine.medical_treatmentMolecular Sequence DataOctopodiformesBiologyBiochemistryEvolution MolecularArchaeogastropodaComplementary DNAmedicineAnimalsProtein IsoformsComputer SimulationAmino Acid SequenceMolecular BiologyPeptide sequencePhylogenyGene LibrarySequence Homology Amino AcidProtein primary structureHemocyaninCell BiologyAnatomybiology.organism_classificationRespiratory proteinBiochemistryMolluscaHemocyaninsProtein BindingJournal of Biological Chemistry
researchProduct

cDNA Cloning and Functional Expression of Jerdostatin, a Novel RTS-disintegrin from Trimeresurus jerdonii and a Specific Antagonist of the α1β1 Integ…

2005

Jerdostatin represents a novel RTS-containing short disintegrin cloned by reverse transcriptase-PCR from the venom gland mRNA of the Chinese Jerdons pit viper Trimeresurus jerdonii. The jerdostatins precursor cDNA contained a 333-bp open reading frame encoding a signal peptide, a pre-peptide, and a 43-amino acid disintegrin domain, whose amino acid sequence displayed 80% identity with that of the KTS-disintegrins obtustatin and viperistatin. The jerdostatin cDNA structure represents the first complete open reading frame of a short disintegrin and points to the emergence of jerdostatin from a short-coding gene. The different residues between jerdostatin and obtustatin/viperistatin are segreg…

Models MolecularSignal peptideProtein FoldingDNA ComplementaryMagnetic Resonance SpectroscopyProtein ConformationDisintegrinsMolecular Sequence DataIntegrinMutantGene ExpressionPeptide MappingBiochemistryIntegrin alpha1beta1Open Reading FramesExocrine GlandsComplementary DNACrotalid VenomsDisintegrinAnimalsTrimeresurusTrypsinAmino Acid SequenceCysteineDisulfidesCloning MolecularMolecular BiologyPeptide sequenceMessenger RNABase SequencebiologyCell BiologyMolecular biologyRecombinant ProteinsOpen reading frameMutagenesis Site-Directedbiology.proteinJournal of Biological Chemistry
researchProduct

Addition of a signal peptide sequence to theα1D-adrenoceptor gene increases the density of receptors, as determined by [3H]-prazosin binding in the m…

2005

1 Both in mammalian tissues and in transfected cells, only low levels of α1D-adrenoceptors are detected in radioligand binding studies. It has been implicated that the comparatively long N-terminal tail of the α1D-adrenoceptor is responsible for the inefficient surface expression of the receptor. 2 In the present study, we created gene constructs for six N-terminally truncated variants of the human α1D-adrenoceptor. These constructs were used to transfect Neuro2A cells. We show that the density of α1D-adrenoceptors, observed by [3H]-prazosin binding, gradually increased with longer truncations of the N-terminus. This seems to indicate that the long N-terminal tail nonspecifically interferes…

Pharmacologychemistry.chemical_classificationSignal peptideTransfectionBiologyCell biologyTransmembrane domainBiochemistrychemistryDownregulation and upregulationBinding siteInositol phosphateReceptorPeptide sequenceBritish Journal of Pharmacology
researchProduct

The membrane anchor of microsomal epoxide hydrolase from human, rat, and rabbit displays an unexpected membrane topology.

1997

The microsomal epoxide hydrolase (mEH) and cytochrome P450s catalyze the sequential formation of carcinogenic metabolites. According to one algorithm for predicting the membrane topology of proteins, the human, the rabbit, and the rat mEH should adopt a type II topology. The type II topology is also predicted by a recently established neuronal network which is trained to recognize signal peptides with very high accuracy. In contrast to these predictions we find, based on N-glycosylation analysis in a cell-free and in a cellular system, that the membrane anchor of human, rat, and rabbit mEH displays a type I topology. This result is correctly predicted by the positive inside rule in which ne…

Signal peptide1303 BiochemistryGlycosylationGlycosylationCytochromeStereochemistryRecombinant Fusion ProteinsImmunoblottingMolecular Sequence DataBiophysics10050 Institute of Pharmacology and Toxicology610 Medicine & healthProtein Sorting SignalsTransfectionBiochemistry1307 Cell BiologyCell membranechemistry.chemical_compoundSpecies Specificity1312 Molecular BiologymedicineElectrochemistryAnimalsHumansAmino Acid SequenceMolecular BiologyPeptide sequenceEpoxide HydrolasesbiologyCell MembraneCell BiologyRatsmedicine.anatomical_structurechemistryMutagenesisMicrosomal epoxide hydrolaseMembrane topologyEpoxide HydrolasesCOS Cellsbiology.protein570 Life sciences; biologyRabbits1304 BiophysicsBiochemical and biophysical research communications
researchProduct