Search results for " Regulation"

showing 10 items of 3187 documents

Subunits composition and allosteric control in Carcinus aestuarii hemocyanin

1998

Carcinus aestuarii hemocyanin (Hc) exists in two aggregation forms at pH 7.5 and 20 mM Ca2+: 24S accounting for 90% of total hemocyanin and 16S accounting for 10%. Removal of metal cations by EDTA at neutral pH causes the complete dissociation of 24S hemocyanin into two different 16S. At pH 9.2, 24S hemocyanin dissociates into a pH stable 16S and a 5S component. The 5S component consists of three monomeric fractions named CaeSS1 (10%), CaeSS2 (50%) and CaeSS3 (40%); the latter fraction consisting of two isoforms. The fractions CaeSS1, CaeSS2 and CaeSS3 have been studied as far as their reassociation properties to form hexamers are concerned. We investigated the oxygen-binding properties of …

Protein ConformationStereochemistrymedicine.medical_treatmentProtein subunitAllosteric regulationHemocyaninBiochemistryAllosteric interactionchemistry.chemical_compoundProtein structureOxygen bindingAllosteric RegulationCrustaceaMetalloproteinsmedicineMetalloproteinAnimalschemistry.chemical_classificationHemocyanin; Oxygen binding; Allosteric interaction; OxygenbiologyHemocyaninHydrogen-Ion Concentrationbiology.organism_classificationOxygenCarcinus aestuariiMonomerBiochemistrychemistryHemocyaninsChromatography GelElectrophoresis Polyacrylamide GelOxygen bindingProtein Binding
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Allosteric Models for Multimeric Proteins:  Oxygen-Linked Effector Binding in Hemocyanin

2005

In many crustaceans, changing concentrations of several low molecular weight compounds modulates hemocyanin oxygen binding, resulting in lower or higher oxygen affinities of the pigment. The nonphysiological effector caffeine and the physiological modulator urate, the latter accumulating in the hemolymph of the lobster Homarus vulgaris during hypoxia, increase hemocyanin oxygen affinity and decrease cooperativity of oxygen binding. To derive a model that describes the mechanism of allosteric interaction between hemocyanin and oxygen in the presence of urate or caffeine, studies of oxygen, urate, and caffeine binding to hemocyanin were performed. Exposure of lobster hemocyanin to various pH …

Protein Conformationmedicine.medical_treatmentAllosteric regulationchemistry.chemical_elementCooperativityCalorimetryBiochemistryOxygenAllosteric RegulationCaffeineHemolymphmedicineAnimalsBinding siteHypoxiaBinding SitesIsothermal titration calorimetryHemocyaninNephropidaeUric AcidOxygenModels ChemicalBiochemistrychemistryHemocyaninsOxygen bindingProtein BindingBiochemistry
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Curcumin Affects HSP60 Folding Activity and Levels in Neuroblastoma Cells.

2020

The fundamental challenge in fighting cancer is the development of protective agents able to interfere with the classical pathways of malignant transformation, such as extracellular matrix remodeling, epithelial−mesenchymal transition and, alteration of protein homeostasis. In the tumors of the brain, proteotoxic stress represents one of the main triggering agents for cell transformation. Curcumin is a natural compound with anti-inflammatory and anti-cancer properties with promising potential for the development of therapeutic drugs for the treatment of cancer as well as neurodegenerative diseases. Among the mediators of cancer development, HSP60 is a key factor for the maintenance of…

Protein FoldingCurcuminCell SurvivalCellCatalysisMalignant transformationCell Linelcsh:ChemistryInorganic ChemistryMitochondrial Proteinschemistry.chemical_compoundNeuroblastomaDownregulation and upregulationHeat shock proteinmedicinepost-translational modificationsHumansSecretionPhysical and Theoretical Chemistrylcsh:QH301-705.5Molecular BiologySpectroscopyCell ProliferationHeat shock proteinDose-Response Relationship DrugCommunicationOrganic Chemistrymolecular chaperonesUbiquitinationGeneral MedicineChaperonin 60Computer Science ApplicationsCell biologyUp-RegulationBrain tumorGene Expression Regulation Neoplasticmedicine.anatomical_structurelcsh:Biology (General)lcsh:QD1-999chemistryApoptosisheat shock proteinsMolecular chaperoneCurcuminbrain tumorsHSP60Post-translational modificationHSP60extracellular HSP60International journal of molecular sciences
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RNA-binding ability of PIPP in requires the entire protein

2003

Post-transcriptional fate of eukaryotic mRNAs depends on association with different classes of RNA-binding proteins (RBPs). Among these proteins, the cold-shock domain (CSD)-containing proteins, also called Y-box proteins, play a key role in controlling the recruitment of mRNA to the translational machinery, in response to environmental cues, both in development and in differentiated cells. We recently cloned a rat cDNA encoding a new CSD-protein that we called PIPPin. This protein also contains two putative double-stranded RNA-binding motifs (PIP(1) and PIP(2)) flanking the central CSD, and is able to bind mRNAs encoding H1 degrees and H3.3 histone variants. In order to clarify the role of…

Protein FoldingNerve Tissue ProteinsSequence alignmentRNA-binding proteinPlasma protein bindingArticleRNA-binding proteinscold-shock domainPIPPinhistone variantsHistonesSettore BIO/10 - BiochimicaComplementary DNAHistone H2AAnimalsRNA MessengerGeneticsMessenger RNAbiologyRNA-Binding ProteinsRNACell BiologyRecombinant ProteinsProtein Structure TertiaryRatsCell biologyHistoneGene Expression Regulationbiology.proteinMolecular MedicineSequence AlignmentProtein BindingJournal of Cellular and Molecular Medicine
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Complementation of Saccharomyces cerevisiae mutationsin genes involved in translation and protein folding (EFB1 and SSB1)with Candida albicans cloned…

2000

We have demonstrated that the expression of Candida albicans genes involved in translation and protein folding (EFB1 and SSB1) complements the phenotype of Saccharomyces cerevisiae mutants. The elongation factor 1beta (EF-1beta) is essential for growth and efb1 S. cerevisiae null mutant cells are not viable; however, viable haploid cells, carrying the disrupted chromosomal allele of the S. cerevisiae EFB1 gene and pEFB1, were isolated upon sporulation of a diploid strain which was heterozygous at the EFB1 locus and transformed with pEFB1 (a pEMBLYe23 derivative plasmid containing an 8-kb DNA fragment from the C. albicans genome which contains the EFB1 gene). This indicates that the C. albic…

Protein FoldingSaccharomyces cerevisiae ProteinsSaccharomyces cerevisiaeMutantSaccharomyces cerevisiaeMicrobiologyPeptide Elongation Factor 1Transformation GeneticGene Expression Regulation FungalHeat shock proteinCandida albicansProtein biosynthesisHSP70 Heat-Shock ProteinsCandida albicansMolecular BiologyGenebiologyGenetic Complementation TestTemperatureGeneral Medicinebiology.organism_classificationMolecular biologyComplementationProtein BiosynthesisChaperone (protein)Mutationbiology.proteinResearch in Microbiology
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A Membrane-Bound Vertebrate Globin

2011

The family of vertebrate globins includes hemoglobin, myoglobin, and other O(2)-binding proteins of yet unclear functions. Among these, globin X is restricted to fish and amphibians. Zebrafish (Danio rerio) globin X is expressed at low levels in neurons of the central nervous system and appears to be associated with the sensory system. The protein harbors a unique N-terminal extension with putative N-myristoylation and S-palmitoylation sites, suggesting membrane-association. Intracellular localization and transport of globin X was studied in 3T3 cells employing green fluorescence protein fusion constructs. Both myristoylation and palmitoylation sites are required for correct targeting and m…

Protein StructureLipoylationGreen Fluorescent ProteinsMolecular Sequence Datalcsh:MedicineHemeBiochemistryCell membranechemistry.chemical_compoundModel OrganismsPalmitoylationhemic and lymphatic diseasesmedicineAnimalsRespiratory functionAmino Acid SequenceGlobinlcsh:ScienceProtein InteractionsBiologyZebrafishZebrafishMyristoylationHemoproteinsMultidisciplinarySequence Homology Amino Acidbiologylcsh:RCell MembraneMembrane ProteinsProteinsGene Expression Regulation DevelopmentalAnimal Modelsbiology.organism_classificationRecombinant ProteinsGlobinsGlobin foldOxygenmedicine.anatomical_structureBiochemistryMyoglobinchemistryImmunoglobulin GCytochemistrylcsh:QRabbitsResearch ArticleSubcellular FractionsPLoS ONE
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Mutational analyses of YqjA, a Tvp38/DedA protein of E. coli

2015

AbstractMembrane proteins of the DedA/Tvp38 protein family are involved in membrane integrity and virulence of pathogenic organisms. However, the structure and exact function of any member of this large protein family are still unclear. In the present study we analyzed the functional and structural properties of a DedA homolog. Purified YqjA variants from Escherichia coli are detectable in different oligomeric states and specific homo-interaction of YqjA monomers in the membrane were confirmed by formation of a disulfide bond in the C-terminal transmembrane helix. Moreover, alanine scanning mutagenesis exhibited different interaction sites crucial for YqjA activity vs. dimer formation.

Protein familyDNA Mutational AnalysisBiophysicsVirulencelac operonmedicine.disease_causeBiochemistryProtein Structure SecondaryTvp38Structural BiologyEscherichia coliGeneticsmedicineOligomerizationFunctionMolecular BiologyEscherichia coliAlanineChemistryEscherichia coli ProteinsCell MembraneMutagenesisMembrane ProteinsGene Expression Regulation BacterialCell BiologyAlanine scanningTransmembrane domainMembrane proteinBiochemistryDedAMembrane proteinMutationProtein MultimerizationFEBS Letters
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Linked Analysis of Large Cooperative, Allosteric Systems: The Case of the Giant HBL Hemoglobins

2008

Homotropic and heterotropic allosteric interactions are important mechanisms that regulate protein function. These mechanisms depend on the ability of oligomeric protein complexes to adopt different conformations and to transmit conformation-linked signals from one subunit of the complex to the neighboring ones. An important step in understanding the regulation of protein function is to identify and characterize the conformations available to the protein complex. This task becomes increasingly challenging with increasing numbers of interacting binding sites. However, a large number of interacting binding sites allows for high homotropic interactions (cooperativity) and thus represents the m…

Protein functionOrder (biology)BiochemistryHexagonal crystal systemBilayerProtein subunitAllosteric regulationBiophysicsCooperativityBiologyBinding site
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Proteins participating to the post-transcriptional regulation of the mitochondrial cytochrome c oxidase subunit IV via elements located in the 3′UTR

2009

Abstract In developing rat brain cytochrome c oxidase subunit IV (COXIV) expression is also regulated at post-transcriptional level and two 3′UTR-COXIV RNA-binding factors have been identified. Here, we report the enrichment and identification of the factors from just born rat brains by affinity chromatography of biotinylated 3′UTR-COXIV RNA–protein complexes on streptavidin-conjugated paramagnetic particles. We successfully isolated two main proteins of about 86 and 42 kDa, whose sequences were highly attributable to Hsp90 and Actin. The purified proteins maintain RNA-binding ability and specificity for COXIV messenger and, interacting with the 3′UTR, then could negatively modulate mRNA tr…

Protein subunitRNA-binding proteinMitochondrionChromatography AffinityElectron Transport Complex IVMitochondrial ProteinsRats Sprague-DawleySequence Analysis ProteinSerineAnimalsCytochrome c oxidaseHSP90 Heat-Shock ProteinsPhosphorylationPost-transcriptional regulation RNA-binding proteins Mitochondria Cytochrome c oxidase COXIV 3'UTR3' Untranslated RegionsMolecular BiologyPost-transcriptional regulationMessenger RNAbiologyThree prime untranslated regionBrainRNA-Binding ProteinsTranslation (biology)Cell BiologyActinsRatsMolecular WeightAnimals NewbornGene Expression RegulationBiochemistrybiology.proteinMolecular MedicineProtein BindingMitochondrion
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Peroxisomal and mitochondrial status of two murine oligodendrocytic cell lines (158N, 158JP): potential models for the study of peroxisomal disorders…

2009

International audience; In some neurodegenerative disorders (leukodystrophies) characterized by myelin alterations, the defect of peroxisomal functions on myelin-producing cells (oligodendrocytes) are poorly understood. The development of in vitro models is fundamental to understanding the physiopathogenesis of these diseases. We characterized two immortalized murine oligodendrocyte cell lines: a normal (158N) and a jimpy (158JP) cell line mutated for the proteolipid protein PLP/DM20. Fluorescence microscopy, flow cytometry, and western blotting analysis allow to identify major myelin proteins (PLP colocalizing with mitochondria; myelin basic protein), oligodendrocyte (CNPase and myelin oli…

Proteolipid protein 1BiochemistryMiceMyelinMESH : PhenylbutyratesperoxisomeIsomerasesMESH : Myelin Basic ProteinsEnoyl-CoA HydrataseCell Line TransformedUltrasonographybiologyMESH : Gene Expression RegulationMESH : Myelin Proteolipid Protein3-Hydroxyacyl CoA DehydrogenasesMESH : Myelin-Associated GlycoproteinMESH : Cell Line TransformedPeroxisomeMESH : Multienzyme ComplexesMESH : OligodendrogliaMESH : Enoyl-CoA HydrataseCatalaseFlow CytometryMESH : 3-Hydroxyacyl CoA DehydrogenasesPhenylbutyratesmitochondriaMyelin-Associated GlycoproteinOligodendrogliamyelinMESH : Antineoplastic Agentsmedicine.anatomical_structureMESH : Microscopy Electron TransmissionBiochemistryACOX1MESH : MitochondriaMESH : Acyl-CoA Oxidase2'3'-Cyclic-Nucleotide PhosphodiesterasesMESH : IsomerasesOxidation-ReductionMyelin ProteinsMESH : Flow CytometryAntineoplastic AgentsPeroxisomal Bifunctional EnzymeStatistics NonparametricMyelin oligodendrocyte glycoproteinCellular and Molecular NeuroscienceMicroscopy Electron TransmissionMultienzyme ComplexesMESH : CatalaseMESH : MicePeroxisomesmedicineAnimalsMESH : ATP-Binding Cassette TransportersMyelin Proteolipid ProteinMESH : Statistics Nonparametric[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyMESH : Oxidation-ReductionMyelin Basic Proteinmurine oligodendrocytesMESH : 2'3'-Cyclic-Nucleotide PhosphodiesterasesPeroxisomal transportOligodendrocyteMyelin basic proteinGene Expression Regulationbiology.proteinATP-Binding Cassette TransportersMyelin-Oligodendrocyte GlycoproteinAcyl-CoA OxidaseMESH : AnimalsMESH : Peroxisomes
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