Search results for "Protein subunit"

showing 10 items of 243 documents

Mass determination, subunit organization and control of oligomerization states of keyhole limpet hemocyanin (KLH).

1997

Analytical dark-field scanning transmission electron microscopy (STEM) of freeze-dried unstained specimens of keyhole limpet hemocyanin (KLH; from Megathura crenulata, a prosobranch gastropod) gave a molecular mass of 400 kDa for the subunit of KLH1 and of 345 kDa for the subunit of KLH2, which confirms our published values from SDS/PAGE. Within the 400-kDa KLH1 subunit we identified, by limited proteolysis, isolation of fragments and N-terminal sequencing, eight distinct 45-60 kDa functional domains (termed 1a through 1h) and determined their sequential arrangement. The KLH1 domains differ biochemically and immunologically from each other and from the previously characterized seven domains…

TrisMicroscopy Electron Scanning TransmissionProtein subunitPopulationMolecular Sequence DataMegathura crenulataBiochemistrychemistry.chemical_compoundAnimalsAmino Acid SequenceeducationMagnesium ionchemistry.chemical_classificationeducation.field_of_studyBinding SitesbiologyMolecular massAnatomybiology.organism_classificationAmino acidMolecular WeightchemistryBiochemistryMolluscaHemocyaninsbiology.proteinKeyhole limpet hemocyaninEuropean journal of biochemistry
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Examination of Escherichia coli from poultry for selected adhesin genes important in disease caused by mammalian pathogenic E. coli

2001

A collection of 1601 extraintestinal and intestinal Escherichia coli isolated from chickens, turkeys and ducks, in Belgium, France and Spain, was hybridised with gene probes specific for fimbrial and afimbrial adhesins (F17, F18, SSfa/F1C, Bfp, Afa, Cs31A, IntiminEae, Aida-1) of intestinal, urinary and invasive E. coli of mammals and with a probe specific for the P (Pap/Prs) fimbrial adhesin of urinary and invasive E. coli of mammals and birds. Three hundred and eighty-three strains (23.9%) were P-positive, 76 strains (4.8%) were Afa-positive, 75 strains (4.7%) were F17-positive, 67 strains (4.2%) were S-positive, 23 (1.4%) were Intimin-positive, and all were F18-, Cs31A-, Aida1- and Bfp-ne…

TurkeysGenotype[SDV]Life Sciences [q-bio]Protein subunitSONDE NUCLEIQUEmedicine.disease_causePolymerase Chain ReactionMicrobiologyMicrobiology03 medical and health sciencesBelgiumTECHNIQUE PCREscherichia colimedicineAnimalsAdhesins BacterialEscherichia coliGeneComputingMilieux_MISCELLANEOUSEscherichia coli InfectionsPoultry Diseases030304 developmental biologyIntimin0303 health sciencesGeneral Veterinarybiology030306 microbiologyGenetic variantsGeneral Medicinebiology.organism_classificationVirologyEnterobacteriaceae[SDV] Life Sciences [q-bio]Bacterial adhesinDucksSpainFimbriae BacterialFranceDNA ProbesChickensBacteriaVeterinary Microbiology
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Allosterism of Nautilus pompilius hemocyanin as deduced from 8 Å cryo-EM structures obtained under oxy and deoxy conditions

2008

Hemocyanins are the blue copper-containing respiratory proteins of many molluscs. Nautilus pompilius hemocyanin (NpH) is a cylindrical decamer composed of ten copies of a 350 kDa polypeptide subunit, in turn consisting of seven O2-binding functional units (FUs, termed NpH-a to NpH-g). Ten copies of the subunit segment NpH-a to NpH-f form the cylinder wall (ca. 35 nm in diameter), whereas the ten copies of NpH-g build the internal collar. Recently we published a 9A cryo-EM structure and molecular model of NpH that solved the principal architecture of this protein [1]. Hemocyanins are highly allosteric, and the cooperativity of oxygen binding should be transferred between functional units by …

Turn (biochemistry)CrystallographyMolecular modelCryo-electron microscopyProtein subunitmedicine.medical_treatmentmedicineCooperativityHemocyaninContext (language use)AnatomyBiologyOxygen binding
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3'-Untranslated regions of oxidative phosphorylation mRNAs function in vivo, as enhancers of translation

2000

Recent findings have indicated that the 3´-untranslated region (3´-UTR) of the mRNA encoding the β-catalytic subunit of the mitochondrial H+-ATP synthase has an in vitro translation-enhancing activity (TEA) [Izquierdo and Cuezva, Mol. Cell. Biol. (1997) 17, 5255–5268; Izquierdo and Cuezva, Biochem. J. (2000) 346, 849–855]. In the present work, we have expressed chimaeric plasmids that encode mRNA variants of green fluorescent protein in normal rat kidney and liver clone 9 cells to determine whether the 3´-UTRs of nuclear-encoded mRNAs involved in the biogenesis of mitochondria have an intrinsic TEA. TEA is found in the 3´-UTR of the mRNAs encoding the α- and β-subunits of the rat H+-ATP syn…

Untranslated regionTranscription GeneticProtein subunitBlotting WesternGreen Fluorescent ProteinsMitochondrionKidneyTransfectionBiochemistryOxidative PhosphorylationCell LineElectron Transport Complex IVMitochondrial ProteinsMitochondrial transcription factor AGenes ReporterAnimalsCytochrome c oxidaseGreen fluorescent proteinRNA MessengerEnhancer3' Untranslated RegionsMolecular BiologyCell NucleusAU-rich elementMessenger RNAbiologyThree prime untranslated regionNuclear ProteinsCell BiologyH+-ATP synthaseMolecular biologyRatsMitochondriaDNA-Binding ProteinsLuminescent ProteinsProton-Translocating ATPasesLiverMicroscopy FluorescenceProtein Biosynthesisbiology.proteinElectrophoresis Polyacrylamide GelResearch ArticlePlasmidsTranscription FactorsCytochrome c oxidase
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A critical role for VEGF and VEGFR2 in NMDA receptor synaptic function and fear-related behavior

2016

Vascular endothelial growth factor (VEGF) is known to be required for the action of antidepressant therapies but its impact on brain synaptic function is poorly characterized. Using a combination of electrophysiological, single-molecule imaging and conditional transgenic approaches, we identified the molecular basis of the VEGF effect on synaptic transmission and plasticity. VEGF increases the postsynaptic responses mediated by the N-methyl-D-aspartate type of glutamate receptors (GluNRs) in hippocampal neurons. This is concurrent with the formation of new synapses and with the synaptic recruitment of GluNR expressing the GluN2B subunit (GluNR-2B). VEGF induces a rapid redistribution of Glu…

Vascular Endothelial Growth Factor A0301 basic medicine[SDV]Life Sciences [q-bio]Cell Culture TechniquesNonsynaptic plasticityBiologyNeurotransmissionHippocampusReceptors N-Methyl-D-AspartateSynaptic TransmissionMice03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicinePostsynaptic potentialAnimalsddc:610Molecular BiologyComputingMilieux_MISCELLANEOUSNeuronsNeuronal PlasticityBehavior AnimalGlutamate receptorExcitatory Postsynaptic PotentialsKinase insert domain receptorFearVascular Endothelial Growth Factor Receptor-2Protein SubunitsPsychiatry and Mental health030104 developmental biologySynaptic fatigueReceptors GlutamateSynapsesSynaptic plasticityNMDA receptorOriginal ArticleNeuroscience030217 neurology & neurosurgery
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Vitamin A deficiency alters rat lung alveolar basement membrane: reversibility by retinoic acid.

2010

Vitamin A is essential for lung development and pulmonary cell differentiation and its deficiency results in alterations of lung structure and function. Basement membranes (BMs) are also involved in those processes, and retinoic acid, the main biologically active form of vitamin A, influences the expression of extracellular matrix macromolecules. Therefore, we have analyzed the ultrastructure and collagen content of lung alveolar BM in growing rats deficient in vitamin A and the recovering effect of all-trans retinoic acid. Male weanling pups were fed a retinol-adequate or -deficient diet until they were 60 days old. A group of vitamin A-deficient pups were recovered by daily intraperitonea…

VitaminCollagen Type IVMalemedicine.medical_specialtymedicine.drug_classEndocrinology Diabetes and MetabolismClinical BiochemistryRetinoic acidTretinoinBiochemistryBasement MembraneCollagen Type ITransforming Growth Factor beta1chemistry.chemical_compoundInternal medicineMalondialdehydemedicineAnimalsRetinoidRNA MessengerRats WistarMolecular BiologyLungPeroxidaseBasement membraneNutrition and DieteticsLungbiologyTumor Necrosis Factor-alphaVitamin A DeficiencyInterleukinsRetinolmedicine.diseaseImmunohistochemistryRatsVitamin A deficiencyPulmonary AlveoliOxidative StressProtein SubunitsEndocrinologymedicine.anatomical_structurechemistryGene Expression RegulationMyeloperoxidasebiology.proteinThe Journal of nutritional biochemistry
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The Largest Subunit of RNA Polymerase II as a New Marker Gene to Study Assemblages of Arbuscular Mycorrhizal Fungi in the Field

2014

Due to the potential of arbuscular mycorrhizal fungi (AMF, Glomeromycota) to improve plant growth and soil quality, the influence of agricultural practice on their diversity continues to be an important research question. Up to now studies of community diversity in AMF have exclusively been based on nuclear ribosomal gene regions, which in AMF show high intra-organism polymorphism, seriously complicating interpretation of these data. We designed specific PCR primers for 454 sequencing of a region of the largest subunit of RNA polymerase II gene, and established a new reference dataset comprising all major AMF lineages. This gene is known to be monomorphic within fungal isolates but shows an…

[SDV]Life Sciences [q-bio]lcsh:MedicineDNA barcodinglaw.inventionGlomeromycotaPlant MicrobiologylawMycorrhizaeCommunity Assemblylcsh:SciencePolymerase chain reactionPhylogenyGeneticsPrincipal Component AnalysisMultidisciplinaryEcologycroissance des plantesFungal geneticsAgricultureBiodiversityExonsSoil EcologyCommunity Ecology[SDE]Environmental SciencesRNA Polymerase IIResearch ArticleSequence analysisGenes FungalMolecular Sequence DataSoil ScienceMycologyBiologychampignon mycorhizienMarker geneMicrobiologyZea mayspcrMutualismBotany[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyDNA Barcoding TaxonomicGlomeromycotalcsh:RfungiEcology and Environmental SciencesBiology and Life SciencesRibosomal RNAbiology.organism_classificationSpecies InteractionsProtein SubunitsPyrosequencinglcsh:QMycorrhizaAgronomic Ecologyqualité du solAgroecologyPLoS ONE
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ISOLATION OF CYTOCHROME OXIDASE COMPLEX FROM SEA URCHIN MITOCHONDRIAL INNER MEMBRANES

1996

Cytochrome oxidase complex has been isolated and purified from sea urchin mitochondrial inner membranes. The complex exhibited a discrete number of bands in PAGE and a 17 kDa band was recognized by an anti-human subunit IV antibody. No bands were recognized by an anti-yeast hsp60 antibody and an anti-sea urchin β ATPase subunit.

animal structuresProtein subunitATPaseCell BiologyGeneral MedicineMitochondrionBiologyMolecular biologyMembraneBiochemistrybiology.animalembryonic structuresbiology.proteinCytochrome c oxidaseHSP60AntibodySea urchinCell Biology International
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Anchorage of Candida albicans Ssr1 to the cell wall, and transcript profiling of the null mutant.

2005

Incorporation into the wall of Candida albicans Ssr1, a GPI-dependent protein, was investigated by construction of different truncated genes for which the three potential omega sites (S199, S215 and G216) and the corresponding omega+1 and omega+2 were eliminated or modified. Cells of the C. albicans ssr1Delta mutant were transformed with pADH-pl harboring the truncated versions of CaSSR1, pADH-DeltaCaSSR1t(217-234) (lacking a C-terminal hydrophobic stretch of 18 aa including the putative omega+2 and omega+1, omega+2 of S215 and G216) or pADH-DeltaCaSSR1t(199-201) (lacking three serine residues), and their walls were analyzed for the protein. Results suggested that the three serine residues …

beta-GlucansTranscription GeneticProtein subunitMutantMolecular Sequence DataMicrobiologySerineFungal ProteinsTranscription (biology)Cell WallCandida albicansCell AdhesionAmino Acid SequenceRNA MessengerCandida albicansMolecular BiologyGeneZinc fingerbiologyGene Expression ProfilingRNA FungalGeneral Medicinebiology.organism_classificationMolecular biologyCorpus albicansCulture MediaGene DeletionProtein BindingResearch in microbiology
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8 Å cryo-EM structure of the giant hemoglobin from the planorbid snail Biomphalaria glabrata

2008

Until 2006, snail red hemoglobin remained a phylogenetic enigma because it occurs quite isolated in a single gastropod family, the Planorbidae, whereas all other gastropods use blue hemocyanin as a respiratory protein (for recent cryo-EM of hemocyanin, see [1,2]). Moreover, sequence data on this snail hemoglobin were completely lacking. In 2006, our group published the complete cDNA and predicted amino acid sequence of two Biomphalaria glabrata hemoglobin polypeptides, termed BgHb1 and BgHb2 [3]. (Biomphalaria is intermediate host of the human parasite Schistosoma mansoni that causes Bilharziosis.) Resembling pearl-chains, both polypeptide subunits encompass 13 different, cysteine-free glob…

biologyChemistrymedicine.medical_treatmentProtein subunitBiomphalariaHemocyaninbiology.organism_classificationRespiratory proteinBiochemistryparasitic diseasesHemolymphmedicineBiomphalaria glabrataGlobinHemoglobin
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