Search results for "Complementary"

showing 10 items of 1156 documents

Molecular cloning and primary structure of a Rhesus (Rh)-like protein from the marine sponge Geodia cydonium

1997

In humans, the 30,000 M(r) Rhesus (Rh) polypeptide D (RhD) is a dominant antigen (Ag) of the Rh blood group system. To date, an Rh-like protein has been found in chimpanzees, gorillas, gibbons, and rhesus monkeys. Related to the 30,000 M(r) Rh Ag protein are two polypeptides of 50,000 M(r), the human 50,000 M(r) Rh Ag and the RhD-like protein from Caenorhabditis elegans. The function of all these proteins is not sufficiently known. Here we characterize a cDNA clone (GCRH) encoding a putative 57,000 M(r) polypeptide from the marine sponge Geodia cydonium, which shares sequence similarity both to the RhD Ag and the Rh50 glycoprotein. The sponge Rh-like protein comprises 523 aa residues; hydro…

Signal peptideDNA ComplementaryMolecular Sequence DataImmunologyMolecular cloningGeneticsAnimalsHumansAmino Acid SequenceCloning MolecularCaenorhabditis elegansGlycoproteinschemistry.chemical_classificationRh-Hr Blood-Group SystemBase SequenceSequence Homology Amino AcidbiologyProtein primary structurebiology.organism_classificationMolecular biologyPoriferaSpongeTransmembrane domainchemistryGlycoproteinRh blood group systemImmunogenetics
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Complete sequence, expression and evolution of two members of the hexamerin protein family during the larval development of the rice moth, Corcyra ce…

2002

Three distinct types of storage hexamerins are expressed in the "last-instar" larvae of the rice moth, Corcyra cephalonica. A cDNA expression library was constructed from fat body-RNA and screened with a polyclonal antibody raised against purified hexamerin (SP2) of Corcyra cephalonica. Two slightly different "full-length" hexamerin cDNA clones (Hex2a and Hex2b) were isolated and sequenced. Both include open reading frames of 2109 bp which are translated into polypeptides of 703 amino acids with 92.5% identity. Signal peptides of 19 amino acids are present at the N-termini. The 684 amino acids native proteins have a high content of aryl groups (17.6%). According to both the criteria for ami…

Signal peptideDNA ComplementaryProtein familyBlotting WesternMolecular Sequence DataMothsBiochemistryEvolution MolecularComplete sequenceComplementary DNAEscherichia coliAnimalsAmino Acid SequenceMolecular BiologyGenePhylogenychemistry.chemical_classificationBase SequenceSequence Homology Amino AcidbiologyfungiBlotting Northernbiology.organism_classificationRecombinant ProteinsAmino acidOpen reading framechemistryBiochemistryRice mothLarvaInsect ScienceInsect ProteinsInsect Biochemistry and Molecular Biology
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mp23, a Theileria parva transmembrane protein with homology to the protein disulfide isomerase family

2002

The protozoan parasite Theileria parva (Apicomplexa) causes the bovine disease East Coast Fever in endemic areas in Subsaharan Africa. The intralymphocytic schizont stage is largely responsible for the pathogenicity and induces a transformed phenotype in host cells [1]. Current evidence supports a model in which the schizont perturbs the immune response by inducing production of cytokines and stimulating the growth of parasitized cells [2]. We were interested to identify parasite proteins involved in parasite/host interaction and have described earlier a screening procedure for identification of schizont stage-exported proteins based on cell-free expression of cDNA and testing for transloca…

Signal peptideDNA ComplementarySequence Homology Amino AcidcDNA libraryEndoplasmic reticulumTheileria parvaMolecular Sequence DataProtein Disulfide-IsomerasesProtozoan ProteinsMembrane ProteinsSequence Analysis DNABiologyTheileria parvabiology.organism_classificationMolecular biologyTransmembrane proteinMembrane proteinComplementary DNAparasitic diseasesAnimalsParasitologyAmino Acid SequenceProtein disulfide-isomeraseMolecular BiologyMolecular and Biochemical Parasitology
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A novel cell wall protein specific to the mycelial form of Yarrowia lipolytica.

1996

A cDNA clone specifying a cell wall protein was isolated from a Yarrowia lipolytica cDNA library. The cDNA library was constructed in the expression vector lambda gt 11, with the RNA isolated from actively growing mycelial cells. The deduced amino acid sequence shows that the encoded protein contains an N-terminal hydrophobic signal peptide. We have designated this protein YWP1 for Yarrowia lipolytica cell Wall Protein. Northern hybridization identified YWP1 transcript only when Y. lipolytica was growing in the mycelial form. The encoded protein seems to be covalently bound to the glucan cell wall since it is not released from the cell walls by sodium dodecyl sulphate extraction, but it is …

Signal peptideDNA ComplementaryTranscription GeneticHydrolasesBlotting WesternGenetic VectorsMolecular Sequence DataRestriction MappingBioengineeringApplied Microbiology and BiotechnologyBiochemistryCell wallFungal ProteinsOpen Reading FramesTransformation GeneticCell WallComplementary DNAGene Expression Regulation FungalYeastsGeneticsEscherichia coliAmino Acid SequenceCloning MolecularFluorescent Antibody Technique IndirectPeptide sequenceAntibodies FungalGene LibraryExpression vectorbiologyBase SequencecDNA libraryRNASodium Dodecyl SulfateYarrowiaRNA Fungalbiology.organism_classificationBlotting NorthernBlotting SouthernBiochemistrySaccharomycetalesElectrophoresis Polyacrylamide GelBiotechnologyYeast (Chichester, England)
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Diplopod hemocyanin sequence and the phylogenetic position of the Myriapoda

2001

Hemocyanins are copper-containing respiratory proteins of the Arthropoda that have so far been thoroughly investigated only in the Chelicerata and the Crustacea but have remained unstudied until now in the Myriapoda. Here we report the first sequence of a myriapod hemocyanin. The hemocyanin of Spirostreptus sp. (Diplopoda: Spirostreptidae) is composed of two distinct subunits that are arranged in a 6 x 6 native molecule. The cloned hemocyanin subunit cDNA codes of for a polypeptide of 653 amino acids (75.5 kDa) that includes a signal peptide of 18 amino acids. The sequence closely resembles that of the chelicerate hemocyanins. Molecular phylogenetic analyses reject with high statistical con…

Signal peptideDNA Complementarymedicine.medical_treatmentMolecular Sequence DataMyriapodachemical and pharmacologic phenomenaBiologycomplex mixturesEvolution MolecularSequence Analysis ProteinGeneticsmedicineAnimalsAmino Acid SequenceCloning MolecularMolecular BiologyArthropodsEcology Evolution Behavior and SystematicsPhylogenyPhylogenetic treeSequence Homology Amino Acidhemic and immune systemsHemocyaninAnatomySequence Analysis DNAbiology.organism_classificationSpirostreptusSister groupEvolutionary biologyHemocyaninsChelicerataSequence AlignmentSpirostreptidae
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The nucleotide and deduced amino acid structures of sheep and pig fetuin. Common structural features of the mammalian fetuin family

1992

This study was initiated to gain further insight into the structural features of the mammalian fetuin family. The cDNA structures of sheep and pig fetuin were determined. The cDNA insert encoding sheep (pig) fetuin comprised 1550 (1470) nucleotides, including 54 (46) nucleotides encoding a signal peptide of 18 (15) residues and 1038 (1041) nucleotides encoding the 346 (347) amino acids of the mature plasma protein. The predicted amino-terminal sequence of the mature pig fetuin was confirmed by the amino-terminal sequence of the purified protein. However, two alternative sheep amino-terminal sequences were found in fetuin purified from the plasma of a single sheep fetus; the minor product wa…

Signal peptideGlycosylationSwineBlotting WesternMolecular Sequence DataSequence alignmentBiologyBiochemistrySequence Homology Nucleic AcidComplementary DNAEndopeptidasesAnimalsHumansAmino Acid SequenceCloning MolecularPeptide sequenceMammalschemistry.chemical_classificationSheepBase SequenceSerine EndopeptidasesStructural geneNucleic acid sequenceMembrane ProteinsDNAMolecular biologyFetuinAmino acidBiochemistrychemistryElectrophoresis Polyacrylamide Gelalpha-FetoproteinsEuropean Journal of Biochemistry
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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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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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Isolation and characterization of two T-box genes from sponges, the phylogenetically oldest metazoan taxon

2003

It is now well established that all metazoan phyla derived from one common ancestor, the hypothetical Urmetazoa. Due to the basal position of Porifera (Demospongiae) in the phylogenetic tree of Metazoa, studies on the mechanisms controlling the development of these animals can provide clues on the understanding of the origin of multicellular animals and on how the first organization of the body plan evolved. In this report we describe the isolation and genomic characterization of two T-box genes from the siliceous sponge Suberites domuncula. The phylogenetic analysis classifies one into the subfamily of Brachyury, Sd-Bra, and the second into the Tbx2 subfamily, Sd-Tbx2. Analyses of the Sd-B…

Siliceous spongeBrachyuryDNA ComplementarySubfamilyMolecular Sequence DataMolecular evolutionPhylogeneticsGeneticsAnimalsProtein IsoformsElectrophoresis Gel Two-DimensionalAmino Acid SequencePhylogenyBase SequencebiologyPhylogenetic treeSequence Analysis DNAAnatomybiology.organism_classificationPoriferaSuberites domunculaAlternative SplicingBody planEvolutionary biologyT-Box Domain ProteinsProtein Processing Post-TranslationalDevelopmental BiologyDevelopment Genes and Evolution
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