Search results for "Subunit"

showing 10 items of 513 documents

Messenger RNA of the large subunit of ribulose-1,5-bisphosphate carboxylase from Chlamydomonas reinhardi. Isolation and properties.

1979

Polysomes specifically synthesizing the large subunit of ribulose-1,5-bisphosphate carboxylase were isolated from Chlamydomonas reinhardi cells by the indirect immunoprecipitation method. Electrophoretic analysis showed that the immunoprecipitated polysomes were of chloroplast origin. The mRNA coding for the large subunit which was purified from immunoprecipitated polysomes migrated at the 19-S position on sucrose density gradients, and its molecular weight was estimated to be 7.3 x 10(5) by acid-urea/agarose gel electrophoresis. The mRNA was translated in vivo with a cell-free protein-synthesizing system derived from Escherichia coli to give full-length large-subunit polypeptides.

Messenger RNARibulose 15-bisphosphateImmunoprecipitationCarboxy-LyasesProtein subunitRibulose-Bisphosphate CarboxylaseChlamydomonasChlamydomonasBiologybiology.organism_classificationBiochemistryMolecular biologyPyruvate carboxylaseMolecular Weightchemistry.chemical_compoundBiochemistrychemistryPolysomePolyribosomesProtein BiosynthesisAgarose gel electrophoresisEscherichia coliRNA MessengerEuropean journal of biochemistry
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Characterisation of Lymnaea cubensis, L. viatrix and L. neotropica n. sp., the main vectors of Fasciola hepatica in Latin America, by analysis of the…

2007

Although, in the endemic areas throughout the world, human fascioliasis presents varying patterns in its epidemiology, the species of lymnaeid snail that act as intermediate hosts and vectors are always crucial in the transmission of the causative parasites. Species in the Galba/Fossaria group of snails, such as Lymnaea cubensis, L. viatrix var. A ventricosa, L. viatrix var. B elongata and Galba truncatula, appear to be frequently involved in the transmission of Fasciola hepatica in Central and South America, although specific classification within this morphologically and anatomically confusing group is often very difficult. To explore the potential use of molecular analyses in the identif…

Mitochondrial DNA030231 tropical medicineSnailDisease VectorsDNA MitochondrialDNA Ribosomal030308 mycology & parasitology03 medical and health sciences0302 clinical medicinebiology.animalBotanyparasitic diseasesAnimalsRibosomal DNAGalba truncatulaLymnaea0303 health sciencesbiologyPhylogenetic tree[SDV.BID.EVO]Life Sciences [q-bio]/Biodiversity/Populations and Evolution [q-bio.PE]Cytochrome c oxidase subunit ICentral AmericaRibosomal RNAFasciola hepaticaSouth Americabiology.organism_classificationInfectious DiseasesParasitologyTrematoda
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Mitochondrial genome of Suberites domuncula: palindromes and inverted repeats are abundant in non-coding regions.

2007

The 26,300-nucleotide sequence of the mitochondrial DNA (mtDNA) molecule of the demosponge Suberites domuncula (Olivi, 1792), the largest in size yet found in Porifera, has been determined. We describe the second hadromerid sponge mitochondrial genome that contains the same set of 41 genes as the hadromerid sponge Tethya actinia, including trnMe(cau), trnI2(cau), trnR2(ucu), and atp9, all of which are transcribed in the same direction. Furthermore, rRNA genes for the small and large ribosomal subunit are very long, rns is indeed the longest among Metazoa (1833 bp). Intergenic regions (IGR) comprise about 25% of S. domuncula mtDNA and include numerous direct and inverted repeats, as well as …

Mitochondrial DNAInverted repeatMolecular Sequence DataSuberites ficusDNA MitochondrialIntergenic regionRNA TransferSpecies SpecificityLarge ribosomal subunitSequence Homology Nucleic AcidGeneticsAnimalsGenePhylogenyRepetitive Sequences Nucleic AcidGeneticsPorifera ; Hadromerida ; mtDNA ; mitochondrial evolution ; polymorphismsBase CompositionbiologyBase SequenceGenetic VariationGeneral MedicineRibosomal RNAbiology.organism_classificationSuberites domunculaGenome MitochondrialDNA IntergenicSuberitesGene
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Deregulated repression of c-Jun provides a potential link to its role in tumorigenesis.

2004

The transcription factor c-Jun cooperates with oncogenic alleles of ras in malignant transformation. Constitutively active Ras causes, via activation of mitogen activated protein kinases, phosphorylation of c-Jun which is essential for subsequent target gene activation and tumorigenesis. Studying the mechanisms controlling c-Jun activity we found that its transcription activation function is actively repressed by a presumably multimeric repressor complex that includes histone deacetylase 3 as a critical subunit. Suppression of c-Jun is relieved by MAP kinase-mediated phosphorylation and/or titration of inhibitor components. The viral tumorigenic counterpart of c-Jun, v-Jun, escapes this inh…

Mitogen-Activated Protein Kinase KinasesTranscriptional ActivationKinaseProtein subunitc-junCell CycleRepressorCell BiologyBiologyHDAC3Histone DeacetylasesMalignant transformationEnzyme ActivationRepressor ProteinsCell Transformation NeoplasticGenes junCancer researchras ProteinsPhosphorylationAnimalsHumansPhosphorylationMolecular BiologyTranscription factorDevelopmental Biology
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Structure of Rhodococcus erythropolis limonene-1,2-epoxide hydrolase reveals a novel active site

2003

Epoxide hydrolases are essential for the processing of epoxide-containing compounds in detoxification or metabolism. The classic epoxide hydrolases have an alpha/beta hydrolase fold and act via a two-step reaction mechanism including an enzyme-substrate intermediate. We report here the structure of the limonene-1,2-epoxide hydrolase from Rhodococcus erythropolis, solved using single-wavelength anomalous dispersion from a selenomethionine-substituted protein and refined at 1.2 A resolution. This enzyme represents a completely different structure and a novel one-step mechanism. The fold features a highly curved six-stranded mixed beta-sheet, with four alpha-helices packed onto it to create a …

Models MolecularAFSG Stafafdelingen (WUATV)10050 Institute of Pharmacology and Toxicologydrug protein bindingEnantioselectivityEpoxide hydrolaseCrystallography X-Rayuncultured actinomyceteCatalytic Domain2400 General Immunology and Microbiologyalpha helixRhodococcuscholesterol epoxide hydrolasenaphthalene 12-dioxygenasedcl14limonene 12 epoxide hydrolaseEpoxide hydrolaseBacteria (microorganisms)delta(5)-3-ketosteroid isomeraseEpoxide HydrolasesLimonene-12-epoxide hydrolaseGeneral Neurosciencearticle2800 General NeuroscienceActinobacteria (class)Articlesagrobacterium-radiobacterEnzyme structureRecombinant Proteinsunclassified drugenzyme structurereaction analysisBiochemistrypriority journalenzyme active siteMechanism2-dioxygenaseDimerizationBiotechnologychemical reactioncrystal structureaspergillus-nigermacromolecular structuresStereochemistrybeta sheetvalpromideMolecular Sequence Data610 Medicine & healthGenetics and Molecular BiologyBiologyGeneral Biochemistry Genetics and Molecular BiologyBacterial Proteinssite directed mutagenesis1300 General Biochemistry Genetics and Molecular BiologyHydrolase1312 Molecular BiologyAmino Acid SequencedetoxificationRhodococcus erythropolisBiologyMonoterpene degradationMolecular Biologyprotein data-bankenzyme substrate complexEnzyme substrate complexnonhumancatalysisSequence Homology Amino AcidGeneral Immunology and Microbiologybacterial enzymeActive sitecrystal-structureAFSG Staff Departments (WUATV)enzyme metabolismProtein SubunitsenzymeEpoxide HydrolasesGeneral Biochemistrybiology.proteinMutagenesis Site-Directed570 Life sciences; biologyselenomethioninenaphthalene 1Alpha helix
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Pharmacological activity of C10-substituted analogs of the high-affinity kainate receptor agonist dysiherbaine

2009

Kainate receptor antagonists have potential as therapeutic agents in a number of neuropathologies. Synthetic modification of the convulsant marine toxin neodysiherbaine A (NDH) previously yielded molecules with a diverse set of pharmacological actions on kainate receptors. Here we characterize three new synthetic analogs of NDH that contain substituents at the C10 position in the pyran ring of the marine toxin. The analogs exhibited high-affinity binding to the GluK1 (GluR5) subunit and lower affinity binding to GluK2 (GluR6) and GluK3 (GluR7) subunits in radioligand displacement assays with recombinant kainate and AMPA receptors. As well, the natural toxin NDH exhibited approximately 100-f…

Models MolecularAgonistKainic acidPatch-Clamp TechniquesTime FactorsStereochemistrymedicine.drug_classProtein subunitGreen Fluorescent ProteinsGlutamic AcidKainate receptorAMPA receptorMolecular Dynamics SimulationLigandsTransfectionTritiumBinding CompetitiveArticleMembrane PotentialsRadioligand AssayStructure-Activity RelationshipCellular and Molecular Neurosciencechemistry.chemical_compoundReceptors Kainic AcidExcitatory Amino Acid AgonistsmedicineRadioligandHumansReceptoralpha-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic AcidCell Line TransformedPharmacologyAlanineKainic AcidDose-Response Relationship DrugMolecular StructureChemistryBridged Bicyclo Compounds HeterocyclicProtein SubunitsBiochemistryMutagenesis Site-DirectedMarine toxinNeuropharmacology
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Full Domain Closure of the Ligand-binding Core of the Ionotropic Glutamate Receptor iGluR5 Induced by the High Affinity Agonist Dysiherbaine and the …

2009

The prevailing structural model for ligand activation of ionotropic glutamate receptors posits that agonist efficacy arises from the stability and magnitude of induced domain closure in the ligand-binding core structure. Here we describe an exception to the correlation between ligand efficacy and domain closure. A weakly efficacious partial agonist of very low potency for homomeric iGluR5 kainate receptors, 8,9-dideoxyneodysiherbaine (MSVIII-19), induced a fully closed iGluR5 ligand-binding core. The degree of relative domain closure, approximately 30 degrees , was similar to that we resolved with the structurally related high affinity agonist dysiherbaine and to that of l-glutamate. The ph…

Models MolecularAgonistStereochemistrymedicine.drug_classGlutamic AcidKainate receptorCrystallography X-RayLigandsBiochemistryPartial agonistCell LineReceptors Kainic AcidmedicineHumansComputer SimulationAmino AcidsReceptorMolecular BiologyAlanineBinding SitesChemistryMechanisms of Signal TransductionGlutamate receptorHydrogen BondingCell BiologyBridged Bicyclo Compounds HeterocyclicLigand (biochemistry)Protein Structure TertiaryProtein SubunitsIonotropic glutamate receptorProtein BindingIonotropic effectJournal of Biological Chemistry
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Functional cysteine-less subunits of the transporter associated with antigen processing (TAP1 and TAP2) by de novo gene assembly

2002

AbstractWithin the adaptive immune system the transporter associated with antigen processing (TAP) plays a pivotal role in loading of peptides onto major histocompatibility (MHC) class I molecules. As a central tool to investigate the structure and function of the TAP complex, we created cysteine-less human TAP subunits by de novo gene synthesis, replacing all 19 cysteines in TAP1 and TAP2. After expression in TAP-deficient human fibroblasts, cysteine-less TAP1 and TAP2 are functional with respect to adenosine triphosphate (ATP)-dependent peptide transport and inhibition by ICP47 from herpes simplex virus. Cysteine-less TAP1 and TAP2 restore maturation and intracellular trafficking of MHC c…

Models MolecularBiophysicsBiological Transport ActiveBiologyMajor histocompatibility complexTransfectionBiochemistryCell Linechemistry.chemical_compoundAdenosine TriphosphateStructural BiologyATP Binding Cassette Transporter Subfamily B Member 3Cysteine-scanning mutagenesisMHC class IGeneticsHumansCysteineATP Binding Cassette Transporter Subfamily B Member 2Molecular BiologyAntigen PresentationAntigen processingHistocompatibility Antigens Class ICell BiologyTransporter associated with antigen processingMolecular biologyRecombinant ProteinsCell biologyProtein SubunitschemistryAmino Acid SubstitutionAntigen processingPeptide transportMembrane proteinbiology.proteinAdenosine triphosphate-binding cassette transporterTAP2ATP-Binding Cassette TransportersTAP1Adenosine triphosphateFEBS Letters
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Design and construction of highly stable, protease-resistant chimeric avidins.

2005

The chicken avidin gene family consists of avidin and seven separate avidin-related genes (AVRs) 1-7. Avidin protein is a widely used biochemical tool, whereas the other family members have only recently been produced as recombinant proteins and characterized. In our previous study, AVR4 was found to be the most stable biotin binding protein thus far characterized (T(m) = 106.4 degrees C). In this study, we studied further the biotin-binding properties of AVR4. A decrease in the energy barrier between the biotin-bound and unbound state of AVR4 was observed when compared with that of avidin. The high resolution structure of AVR4 facilitated comparison of the structural details of avidin and …

Models MolecularBiotin bindingInsectaProtein familyProtein subunitRecombinant Fusion ProteinsMolecular Sequence DataBiotinBiosensing TechniquesBiologyProtein EngineeringBiochemistryProtein Structure SecondaryProtein structureAnimalsAmino Acid SequenceMolecular BiologyThermostabilityCalorimetry Differential ScanningSequence Homology Amino AcidTemperatureCell BiologyProtein engineeringAvidinRecombinant ProteinsProtein Structure TertiaryKineticsBiochemistryMicroscopy FluorescenceMutagenesisBiotinylationMutationbiology.proteinChromatography GelThermodynamicsElectrophoresis Polyacrylamide GelEndopeptidase KBaculoviridaeChickensAvidinChromatography LiquidPeptide HydrolasesProtein BindingThe Journal of biological chemistry
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Introduction of histidine residues into avidin subunit interfaces allows pH-dependent regulation of quaternary structure and biotin binding

2003

AbstractIn order to turn the subunit association and biotin binding of avidin into pH-sensitive phenomena, we have replaced individually three amino acid residues in avidin (Met96, Val115 and Ile117) with histidines in the 1–3 interface, and in combination with a histidine conversion in the 1–2 interface (Trp110). The single replacements Met96His and Val115His in the 1–3 interface were found to have a clear effect on the quaternary structure of avidin, since subunit associations of these mutants became pH-dependent. The histidine replacement in the 1–2 interface affected the biotin-binding properties of the mutants, in particular reversibility of binding and protein–ligand complex formation…

Models MolecularBiotin bindingInsectaProtein subunitBiophysicsBiotinBiosensing TechniquesBiochemistryCell LineProtein structureStructural BiologyGeneticsAnimalsHistidinepH dependenceProtein Structure QuaternaryMolecular BiologyHistidinebiologyChemistryCell BiologyProtein engineeringHydrogen-Ion ConcentrationAvidinRecombinant ProteinsMolecular WeightProtein SubunitsSpectrometry FluorescenceAmino Acid SubstitutionBiochemistryBiotinylationBiophysicsbiology.proteinProtein quaternary structureProtein engineeringBaculoviridaeProtein BindingAvidinFEBS Letters
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