Search results for "Cloning"

showing 10 items of 498 documents

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
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Biochemical characterization and ligand binding properties of neuroglobin, a novel member of the globin family.

2001

Neuroglobin is a recently discovered member of the globin superfamily that is suggested to enhance the O(2) supply of the vertebrate brain. Spectral measurements with human and mouse recombinant neuroglobin provide evidence for a hexacoordinated deoxy ferrous (Fe(2+)) form, indicating a His-Fe(2+)-His binding scheme. O(2) or CO can displace the endogenous protein ligand, which is identified as the distal histidine by mutagenesis. The ferric (Fe(3+)) form of neuroglobin is also hexacoordinated with the protein ligand E7-His and does not exhibit pH dependence. Flash photolysis studies show a high recombination rate (k(on)) and a slow dissociation rate (k(off)) for both O(2) and CO, indicating…

Models MolecularTime FactorsLightStereochemistryIronNeuroglobinNerve Tissue ProteinsPlasma protein bindingLigandsBiochemistryMiceAnimalsHumansHistidineGlobinCloning MolecularMolecular BiologyHistidineChromatography High Pressure LiquidCarbon MonoxideChemistryCytoglobinTemperatureCell BiologyHydrogen-Ion ConcentrationLigand (biochemistry)Recombinant ProteinsGlobin foldGlobinsOxygenKineticsNeuroglobinOxidation-ReductionUltracentrifugationProtein ligandProtein BindingThe Journal of biological chemistry
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Cloning, tissue distribution, pharmacology and three-dimensional modelling of melanocortin receptors 4 and 5 in rainbow trout suggest close evolution…

2004

The rainbow trout (Oncorhynchus mykiss) is one of the most widely used fish species in aquaculture and physiological research. In the present paper, we report the first cloning, 3D (three-dimensional) modelling, pharmacological characterization and tissue distribution of two melanocortin (MC) receptors in rainbow trout. Phylogenetic analysis indicates that these receptors are orthologues of the human MC4 and MC5 receptors. We created 3D molecular models of these rainbow trout receptors and their human counterparts. These models suggest greater divergence between the two human receptors than between their rainbow trout counterparts. The pharmacological analyses demonstrated that ACTH (adreno…

Models Molecularendocrine systemmedicine.medical_specialtyanimal structuresanimal diseasesMolecular Sequence DataAdrenocorticotropic hormoneBiologyKidneyBinding Competitivedigestive systemBiochemistryCell LineEvolution MolecularInternal medicinemedicineAnimalsHumansAmino Acid SequenceCloning MolecularBinding siteReceptorMolecular BiologyPhylogenyPharmacologyCloningBinding Sitesurogenital systemReceptors MelanocortinSequence Analysis DNACell BiologyCell biologyZincEndocrinologyReceptors CorticotropinOrgan SpecificityHypothalamusHormone receptorOncorhynchus mykissReceptor Melanocortin Type 4Rainbow troutMelanocortinSequence AlignmentResearch ArticleBiochemical Journal
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Subunit organization of the abalone Haliotis tuberculata hemocyanin type 2 (HtH2), and the cDNA sequence encoding its functional units d, e, f, g and…

1999

We have developed a HPLC procedure to isolate the two different hemocyanin types (HtH1 and HtH2) of the European abalone Haliotis tuberculata. On the basis of limited proteolytic cleavage, two-dimensional immunoelectrophoresis, PAGE, N-terminal protein sequencing and cDNA sequencing, we have identified eight different 40-60-kDa functional units (FUs) in HtH2, termed HtH2-a to HtH2-h, and determined their linear arrangement within the elongated 400-kDa subunit. From a Haliotis cDNA library, we have isolated and sequenced a cDNA clone which encodes the five C-terminal FUs d, e, f, g and h of HtH2. As shown by multiple sequence alignments, defg of HtH2 correspond structurally to defg from Octo…

Models Molecularfood.ingredientDNA ComplementarySequence analysismedicine.medical_treatmentMolecular Sequence DataOctopodiformesMegathura crenulataBiochemistryEvolution MolecularfoodSequence Analysis ProteinComplementary DNAmedicineAnimalsHaliotisAmino Acid SequenceCloning MolecularProtein Structure QuaternaryPeptide sequenceImmunoelectrophoresisbiologySequence Homology Amino AcidcDNA libraryHelix SnailsProtein primary structureHemocyaninAnatomySequence Analysis DNAbiology.organism_classificationPeptide FragmentsBiochemistryMolluscaHemocyaninsEuropean journal of biochemistry
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The cold shock response of the psychrotrophic bacterium Pseudomonas fragi involves four low-molecular-mass nucleic acid-binding proteins

1997

The psychrotrophic bacterium Pseudomonas fragi was subjected to cold shocks from 30 or 20 to 5 degrees C. The downshifts were followed by a lag phase before growth resumed at a characteristic 5 degrees C growth rate. The analysis of protein patterns by two-dimentional gel electrophoresis revealed overexpression of 25 or 17 proteins and underexpression of 12 proteins following the 30- or 20-to-5 degrees C shift, respectively. The two downshifts shared similar variations of synthesis of 20 proteins. The kinetic analysis distinguished the induced proteins into cold shock proteins (Csps), which were rapidly but transiently overexpressed, and cold acclimation proteins (Caps), which were more or …

Molecular Sequence DataAdaptation BiologicalBiologyMicrobiologyPolymerase Chain Reaction03 medical and health sciencesHeat acclimationBacterial ProteinsPseudomonas fragiHeat shock proteinNucleic AcidsPseudomonasCold acclimationElectrophoresis Gel Two-DimensionalAmino Acid SequenceCloning MolecularMolecular BiologyPeptide sequence[SDV.MP] Life Sciences [q-bio]/Microbiology and ParasitologyHeat-Shock ProteinsComputingMilieux_MISCELLANEOUS030304 developmental biologyGel electrophoresis0303 health sciencesBase SequenceSequence Homology Amino Acid030306 microbiologySequence Analysis DNACold-shock domainbiology.organism_classificationMolecular biologyCold shock responseCold TemperatureDNA-Binding Proteins[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyBiochemistryGenes BacterialCarrier ProteinsSequence AnalysisGenome BacterialResearch ArticleProtein Binding
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Molecular Evolution of Apoptotic Pathways: Cloning of Key Domains from Sponges (Bcl-2 Homology Domains and Death Domains) and Their Phylogenetic Rela…

2000

Cells from metazoan organisms are eliminated in a variety of physiological and pathophysiological processes by apoptosis. In this report, we describe the cloning and characterization of molecules from the marine sponges Geodia cydonium and Suberites domuncula, whose domains show a high similarity to those that are found in molecules of the vertebrate Bcl-2 superfamily and of the death receptors. The Bcl-2 proteins contain up to four Bcl-2 homology regions (BH). Two Bcl-2-related molecules have been identified from sponges that are provided with two of those regions, BH1 and BH2, and are termed Bcl-2 homology proteins (BHP). The G. cydonium molecule, BHP1_GC, has a putative size of 28,164, w…

Molecular Sequence DataApoptosisBiologyHomology (biology)Evolution MolecularMolecular evolutionGeneticsAnimalsHumansAnkyrinAmino Acid SequenceCloning MolecularMolecular BiologyGenePhylogenyEcology Evolution Behavior and SystematicsCaenorhabditis eleganschemistry.chemical_classificationGeneticsBase SequenceSequence Homology Amino AcidPhylogenetic treeIntronbiology.organism_classificationPoriferaSuberites domunculaProto-Oncogene Proteins c-bcl-2chemistryPeptidesJournal of Molecular Evolution
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Caspase-mediated apoptosis in sponges: cloning and function of the phylogenetic oldest apoptotic proteases from Metazoa

2003

AbstractSponges (phylum Porifera) represent the phylogenetically oldest metazoan phylum. These animals have complex cell adhesion and powerful immune systems which allow the formation of a distinct body plan. Consequently, an apoptotic machinery has to be predicted that allows sponges to eliminate unwanted cells accumulating during development. With the marine sponge Geodia cydonium, it is shown that allografts of these animals undergo apoptosis as demonstrated by apoptotic DNA fragmentation. Extracts from allografts contain an enzymic activity characteristic for caspases; as substrate to determine the cleavage activity, Ac-DEVD-AMC was applied. cDNAs encoding predicted caspase-3-related pr…

Molecular Sequence DataApoptosisCaspase 3SpongeCoumarinsEndopeptidasesAnimalsInvertebrateAmino Acid SequenceCloning MolecularEnzyme InhibitorsMolecular BiologyPhylogenyCaspasebiologyCaspase 3Cell adhesion moleculeAlternative splicingApoptotic DNA fragmentationPotential proapoptotic molecule DD2Cell BiologyBcl-2 homologous proteinbiology.organism_classificationSuberites domunculaCaspaseCaspase InhibitorsPoriferaCell biologyIsoenzymesSuberites domunculaSpongeApoptosisCaspasesbiology.proteinOligopeptidesSequence AlignmentBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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A multidomain xylanase from a Bacillus sp. with a region homologous to thermostabilizing domains of thermophilic enzymes

1999

The gene xynC encoding xylanase C from Bacillus sp. BP-23 was cloned and expressed in Escherichia coli. The nucleotide sequence of a 3538 bp DNA fragment containing xynC gene was determined, revealing an open reading frame of 3258 bp that encodes a protein of 120,567 Da. A comparison of the deduced amino acid sequence of xylanase C with known beta-glycanase sequences showed that the encoded enzyme is a modular protein containing three different domains. The central region of the enzyme is the catalytic domain, which shows high homology to family 10 xylanases. A domain homologous to family IX cellulose-binding domains is located in the C-terminal region of xylanase C, whilst the N-terminal r…

Molecular Sequence DataBacillusBiologymedicine.disease_causeMicrobiologyHomology (biology)Substrate Specificitychemistry.chemical_compoundCatalytic DomainEnzyme StabilityEscherichia colimedicineXylobioseAmino Acid SequenceCloning MolecularEscherichia coliPeptide sequencechemistry.chemical_classificationEndo-14-beta XylanasesSequence Homology Amino AcidThermophileTemperatureNucleic acid sequenceSequence Analysis DNAXylosidasesEnzymeBiochemistrychemistryGenes BacterialXylanaseSequence AlignmentMicrobiology
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Cytoglobin: A Novel Globin Type Ubiquitously Expressed inVertebrate Tissues

2002

Vertebrates possess multiple respiratory globins that differ in terms of structure, function, and tissue distribution. Three types of globins have been described so far: hemoglobin facilitates the transport of oxygen in the blood, myoglobin serves oxygen transport and storage in the muscle, and neuroglobin has a yet unidentified function in nerve cells. Here we report the identification of a fourth and novel type of globin in mouse, man, and zebrafish. It is expressed in apparently all types of human tissue and therefore has been called cytoglobin (CYGB). Mouse and human CYGBs comprise 190 amino acids; the zebrafish CYGB, 174 amino acids. The human CYGB gene is located on chromosome 17q25. …

Molecular Sequence DataBiologyPolymerase Chain ReactionHemoglobinsMiceExonchemistry.chemical_compoundGeneticsAnimalsHumansTissue DistributionAmino Acid SequenceGlobinCloning MolecularMolecular BiologyGeneZebrafishPhylogenyZebrafishEcology Evolution Behavior and SystematicsDNA PrimersGeneticsSequence Homology Amino AcidCytoglobinCytoglobinOxygen transportExonsBlotting Northernbiology.organism_classificationGlobinsCell biologyMyoglobinchemistryNeuroglobinChromosomes Human Pair 17Molecular Biology and Evolution
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Complex evolution of tandem-repetitive DNA in the Chironomus thummi species group.

1997

The subspecies Chironomus thummi thummi and C. t. piger display dramatic differences in the copy number and chromosomal localization of a tandemly repeated DNA family (Cla elements). In order to analyze the evolutionary dynamics of this repeat family, we studied the organization of Cla elements in the related outgroup species C. luridus. We find three different patterns of Cla element organization in C. luridus, showing that Cla elements may be either strictly tandem-repetitive or be an integral part of two higher-order tandem repeats (i.e., Hinf[lur] elements, Sal[lur] elements). All three types of Cla-related repeats are localized in the centromeres of C. luridus chromosomes. This suggest…

Molecular Sequence DataBiologySubspeciesChironomidaeTransposition (music)Evolution Molecularchemistry.chemical_compoundTandem repeatSpecies SpecificityCentromereGeneticsAnimalsCloning MolecularRepeated sequenceMolecular BiologyEcology Evolution Behavior and SystematicsIn Situ HybridizationRepetitive Sequences Nucleic AcidCloningGeneticsintegumentary systemBase Sequencefood and beveragesDNAchemistryNucleic acidlipids (amino acids peptides and proteins)DNAJournal of molecular evolution
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