Search results for "binding site"

showing 10 items of 856 documents

Differential Regulation of CCL22 Gene Expression in Murine Dendritic Cells and B Cells

2005

Abstract The activated T cell-attracting CC chemokine CCL22 is expressed by stimulated B cells and mature dendritic cells (DC). We have cloned and sequenced the complete mouse gene, including 4 kb of the 5′-flanking promoter region, and detected two distinct sites for initiation of transcription by 5′-RACE. Reporter gene assays indicate that the promoter reflects the specificity of the endogenous gene. Within the proximal promoter region, we identified potential binding sites for NF-κB, Ikaros, and a putative GC box. All three regions bind proteins. The NF-κB site was shown to specifically bind NF-κB subunits p50 and p65 from nuclear extracts of LPS-stimulated B cells, B cell line A20/2J, T…

Transcriptional ActivationSp1 Transcription FactorMolecular Sequence DataImmunologyCAAT boxBiologyCell LineMiceTransactivationGene expressionAnimalsImmunology and AllergyCloning MolecularProtein PrecursorsBinding sitePromoter Regions GeneticGeneChemokine CCL22B-LymphocytesMice Inbred BALB CReporter geneBinding SitesBinding proteinNF-kappa BTranscription Factor RelANF-kappa B p50 SubunitPromoterDendritic CellsMolecular biologyDNA-Binding ProteinsMice Inbred C57BLGene Expression RegulationChemokines CCMutagenesis Site-DirectedNIH 3T3 CellsFemaleTranscription Initiation SiteThe Journal of Immunology
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Transcriptional Regulation of Human CYP3A4 Basal Expression by CCAAT Enhancer-Binding Protein α and Hepatocyte Nuclear Factor-3γ

2003

Cytochrome P450 3A4 (CYP3A4) is involved in the metabolism of more than 50% of currently used therapeutic drugs, yet the mechanisms that control CYP3A4 basal expression in liver are poorly understood. Several putative binding sites for CCAAT/enhancer-binding protein (C/EBP) and hepatic nuclear factor 3 (HNF-3) were found by computer analysis in CYP3A4 promoter. The use of reporter gene assays, electrophoretic mobility shift assays, and site-directed mutagenesis revealed that one proximal and two distal C/EBP alpha binding sites are essential sites for the trans-activation of CYP3A4 promoter. No trans-activation was found in similar reporter gene experiments with a HNF-3 gamma expression vec…

Transcriptional ActivationTranscription GeneticGenetic VectorsBiologyTransfectiondigestive systemGene Expression Regulation EnzymologicChromatin remodelingAdenoviridaeCytochrome P-450 Enzyme SystemCCAAT-Enhancer-Binding Protein-alphamedicineCytochrome P-450 CYP3AHumansEnzyme InhibitorsBinding sitePromoter Regions GeneticCells CulturedPharmacologyReporter geneExpression vectorCcaat-enhancer-binding proteinsNuclear ProteinsMolecular biologyChromatinDNA-Binding ProteinsHistone Deacetylase InhibitorsHepatocyte nuclear factorsTrichostatin AHepatocytesMolecular MedicineHepatocyte Nuclear Factor 3-gammaTranscription Factorsmedicine.drugMolecular Pharmacology
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Physiological activation of the IgH 3' enhancer in B lineage cells is not blocked by Pax-5.

1996

The mouse 3' enhancer contains a high-affinity binding site for the paired box protein Pax-5. Here, we demonstrate by genomic footprinting that the rat 3' enhancer contains a low-affinity binding site for Pax-5, which is occupied in activated splenic B cells. Thus, binding of Pax-5 to the IgH 3' enhancer appears to be evolutionarily conserved in rodents. Analysis of Pax-5 expression in primary B cells demonstrates that Pax-5 remains expressed after 4 days of lipopolysaccharide (LPS) induction, but is down-regulated in 5-day stimulated cells. Similarly, the expression of Pax-5 is down-regulated in vivo in activated large splenocytes, in contrast to small resting cells. Multimerization of the…

Transcriptional Activationcongenital hereditary and neonatal diseases and abnormalitiesanimal structuresImmunologyCD40 LigandDNA FootprintingHeterologousDown-RegulationReceptors Antigen B-CellEnhancer RNAsLymphocyte ActivationMiceGene expressionImmunology and AllergyAnimalsBinding siteEnhancerTranscription factorCells CulturedReporter geneB-LymphocytesCD40Membrane GlycoproteinsbiologyGenes ImmunoglobulinPAX5 Transcription FactorNuclear ProteinsMolecular biologyRatsUp-Regulationbody regionsDNA-Binding ProteinsRepressor ProteinsEnhancer Elements GeneticGene Expression Regulationembryonic structuresbiology.proteinTrans-Activatorssense organsTranscription FactorsEuropean journal of immunology
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Synthetic retinoids dissociate coactivator binding from corepressor release.

2002

The ligand-activated retinoid receptors RXR and RAR control development, homeostasis and disease by regulating transcription of retinoic acid (RA) responsive target genes or crosstalk with other signalling pathways. According to the current model ligand-binding triggers an exchange between corepressor- and coactivator-complexes that inhibit or potentiate transcription by deacetylating and acetylating nucleosomal histones, respectively. Additional cofactors may modify the transcriptional regulatory process by linking liganded retinoid receptors to structural components of chromatin or protein degradation. The desire to specifically influence defined events in RA-signalling, while others are …

Transcriptional Activationmedicine.drug_classReceptors Retinoic AcidAmino Acid MotifsProtein degradationRetinoid X receptorBiologyLigandsBiochemistryRetinoidsCoactivatorChlorocebus aethiopsmedicineAnimalsHumansNuclear Receptor Co-Repressor 1Protein IsoformsNuclear Receptor Co-Repressor 2RetinoidMolecular BiologyNuclear receptor co-repressor 2PELP-1Binding SitesRetinoid X receptor alphaRetinoic Acid Receptor alphaNuclear ProteinsCell BiologyCell biologyDNA-Binding ProteinsRepressor ProteinsBiochemistryGene Expression RegulationCOS CellsMutagenesis Site-DirectedCorepressorHeLa CellsJournal of receptor and signal transduction research
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Structural basis of PETISCO complex assembly during piRNA biogenesis in C. elegans

2021

AbstractPiwi-interacting RNAs (piRNAs) constitute a class of small RNAs that bind PIWI proteins and are essential to repress transposable elements in the animal germline, thereby promoting genome stability and maintaining fertility. C. elegans piRNAs (21U RNAs) are transcribed individually from minigenes as precursors that require 5’ and 3’ processing. This process depends on the PETISCO complex, consisting of four proteins: IFE-3, TOFU-6, PID-3, and ERH-2. We employ biochemical and structural biology approaches to characterize the PETISCO architecture and its interaction with RNA, together with its effector proteins TOST-1 and PID-1. These two proteins define different PETISCO functions: P…

Transposable elementStructural biologyChemistryEffectorProtein subunitGeneticsPiwi-interacting RNARNABiologyBinding siteBiogenesisDevelopmental BiologyCell biologyGenes & Development
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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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Quasispecies dynamics and molecular evolution of human norovirus capsid P region during chronic infection.

2009

In this novel study, we have for the first time identified evolutionarily conserved capsid residues in an individual chronically infected with norovirus (GGII.3). From 2000 to 2003, a total of 147 P1-1 and P2 capsid sequences were sequenced and investigated for evolutionarily conserved and functionally important residues by the evolutionary trace (ET) algorithm. The ET algorithm revealed more absolutely conserved residues (ACR) in the P1-1 domain (47/53, 88 %) as compared with the P2 domain (86/133, 64 %). The capsid P1-1 and P2 domains evolved in time-dependent manner, with a distinct break point observed between autumn/winter of year 2000 (isolates P1, P3 and P5) and spring to autumn of y…

Trisaccharide bindingMolecular Sequence DataViral quasispeciesBiologymedicine.disease_causeEvolution MolecularFecesMolecular evolutionVirologymedicineHumansAmino Acid SequenceCloning MolecularReceptorConserved SequencePhylogenyCaliciviridae InfectionsDNA PrimersImmunosuppression TherapyBinding SitesStrain (chemistry)Reverse Transcriptase Polymerase Chain ReactionNorovirusVirologyChronic infectionCapsidNorovirusBlood Group AntigensRNA ViralCapsid ProteinsSeasonsAlgorithmsThe Journal of general virology
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Purification and spectroscopic studies on catechol oxidases from Lycopus europaeus and Populus nigra: evidence for a dinuclear copper center of type …

1999

We purified two catechol oxidases from Lycopus europaeus and Populus nigra which only catalyze the oxidation of catechols to quinones without hydroxylating tyrosine. The molecular mass of the Lycopus enzyme was determined to 39,800 Da and the mass of the Populus enzyme was determined to 56,050 Da. Both catechol oxidases are inhibited by thiourea, N-phenylthiourea, dithiocarbamate, and cyanide, but show different pH behavior using catechol as substrate. Atomic absorption spectrosopic analysis found 1.5 copper atoms per protein molecule. Using EPR spectroscopy we determined 1.8 Cu per molecule catechol oxidase. Furthermore, EPR spectroscopy demonstrated that catechol oxidase is a copper enzym…

TyrosinaseCatecholschemistry.chemical_elementPhotochemistrySpectrum Analysis RamanBiochemistrylaw.inventionTreesInorganic Chemistrychemistry.chemical_compoundlawPolymer chemistryEnzyme InhibitorsElectron paramagnetic resonanceCatechol oxidaseCatecholBinding SitesCyanidesbiologyMonophenol MonooxygenaseSpectrophotometry AtomicElectron Spin Resonance SpectroscopySubstrate (chemistry)Bridging ligandHydrogen-Ion ConcentrationPlantsPhenylthioureaCopperMolecular WeightchemistryHemocyaninsbiology.proteinSpectrophotometry UltravioletOxygen bindingCatechol OxidaseCopperJournal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry
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PSMA6 (rs2277460, rs1048990), PSMC6 (rs2295826, rs2295827) and PSMA3 (rs2348071) genetic diversity in Latvians, Lithuanians and Taiwanese

2014

PSMA6 (rs2277460, rs1048990), PSMC6 (rs2295826, rs2295827) and PSMA3 (rs2348071) genetic diversity was investigated in 1438 unrelated subjects from Latvia, Lithuania and Taiwan. In general, polymorphism of each individual locus showed tendencies similar to determined previously in HapMap populations. Main differences concern Taiwanese and include presence of rs2277460 rare allele A not found before in Asians and absence of rs2295827 rare alleles homozygotes TT observed in all other human populations. Observed patterns of SNPs and haplotype diversity were compatible with expectation of neutral model of evolution. Linkage disequilibrium between the rs2295826 and rs2295827 was detected to be c…

UPS ubiquitin–proteasome systemLinkage disequilibriumTF transcription factorLD linkage disequilibriumPopulationSNPLocus (genetics)Single-nucleotide polymorphismBiologyArticleHapMap JPT JapaneseGenetic diversityHuman populationTW Taiwanese populationLT Lithuanian populationGeneticsInternational HapMap ProjectAlleleeducationHapMap-CEU NorthWestern EuropeansGenetics (clinical)Geneticseducation.field_of_studyGenetic diversityProteasomeHapMap HCB Han ChineseHWE Hardy–Weinberg equilibriumHaplotypePSMC6LV Latvian populationT2DM type 2 diabetes mellitusPSMA6SNP single nucleotide polymorphismTFBS transcription factor binding sitePSMA3Meta Gene
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NOSIP, a novel modulator of endothelial nitric oxide synthase activity.

2001

Production of nitric oxide (NO) in endothelial cells is regulated by direct interactions of endothelial nitric oxide synthase (eNOS) with effector proteins such as Ca2+-calmodulin, by posttranslational modifications such as phosphorylation via protein kinase B, and by translocation of the enzyme from the plasma membrane caveolae to intracellular compartments. Reversible acylation of eNOS is thought to contribute to the intracellular trafficking of the enzyme; however, protein factor(s) that govern the translocation of the enzyme are still unknown. Here we have used the yeast two-hybrid system and identified a novel 34 kDa protein, termed NOSIP (eNOS interacting protein), which avidly binds …

Ubiquitin-Protein LigasesMolecular Sequence DataCHO CellsCaveolaeBiochemistryNitric oxideSubstrate Specificitychemistry.chemical_compoundEnosCaveolaeCricetinaeTwo-Hybrid System TechniquesGeneticsAnimalsHumansAmino Acid SequenceRNA MessengerMolecular BiologyProtein kinase BCalcimycinBinding SitesbiologyAkt/PKB signaling pathwayGene Expression Profilingbiology.organism_classificationImmunohistochemistryPrecipitin TestsTransport proteinCell biologyNitric oxide synthaseProtein TransportchemistryBiochemistrybiology.proteinEndothelium VascularNitric Oxide SynthaseCarrier ProteinsSequence AlignmentIntracellularBiotechnologyProtein BindingFASEB journal : official publication of the Federation of American Societies for Experimental Biology
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