Search results for "DNA-BINDING PROTEIN"

showing 10 items of 449 documents

Transcriptional Mechanisms of Proneural Factors and REST in Regulating Neuronal Reprogramming of Astrocytes

2015

Summary Direct lineage reprogramming induces dramatic shifts in cellular identity, employing poorly understood mechanisms. Recently, we demonstrated that expression of Neurog2 or Ascl1 in postnatal mouse astrocytes generates glutamatergic or GABAergic neurons. Here, we take advantage of this model to study dynamics of neuronal cell fate acquisition at the transcriptional level. We found that Neurog2 and Ascl1 rapidly elicited distinct neurogenic programs with only a small subset of shared target genes. Within this subset, only NeuroD4 could by itself induce neuronal reprogramming in both mouse and human astrocytes, while co-expression with Insm1 was required for glutamatergic maturation. Cu…

Transcription GeneticRepressorNerve Tissue ProteinsCell fate determinationBiologyDNA-binding proteinArticleMiceGlutamatergicBasic Helix-Loop-Helix Transcription FactorsGeneticsAnimalsHumansPromoter Regions GeneticTranscription factorCells CulturedNeuronsCell BiologyCellular ReprogrammingMolecular biologyCell biologyDNA-Binding ProteinsRepressor ProteinsASCL1Astrocytesembryonic structuresMolecular MedicineGABAergicReprogrammingTranscription FactorsCell Stem Cell
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The Kelch protein NS1-BP interacts with alpha-enolase/MBP-1 and is involved in c-Myc gene transcriptional control

2007

Alpha-enolase is a key glycolytic enzyme that plays a functional role in several physiological processes depending on the cellular localization. The enzyme is mainly localized in the cytoplasm whereas an alternative translated form, named MBP-1, is predominantly nuclear. The MBP-1 protein has been characterized as a c-Myc promoter binding protein that negatively controls transcription. In the present study, we identified the kelch protein NS1-BP as one of the alpha-enolase/MBP-1 partners by using a yeast two-hybrid screening. Although NS1-BP has been originally described as a protein mainly localized in the nucleus, we provide evidence that NS1-BP also interacts with actin in human cells, a…

Transcription GeneticTranscription FactorGlycolysiAlpha-enolaseKelch proteinsRNA-Binding ProteinHeLa CellChlorocebus aethiopsTranscriptional regulationPromoter Regions GeneticCellular localizationNuclear ProteinbiologyNuclear ProteinsRNA-Binding ProteinsCell biologyDNA-Binding ProteinsProtein TransportCOS CellsYeast two-hybrid assayGlycolysisHumanProtein BindingSubcellular FractionsImmunoprecipitationDNA-Binding ProteinTwo-hybrid screeningEnolaseChlorocebus aethiopProto-Oncogene Proteins c-mycCOS CellBiomarkers TumorAnimalsHumansKelch proteinMolecular BiologyActinTumor Suppressor ProteinAnimalTumor Suppressor ProteinsBinding proteinc-Myc transcriptionCell BiologyMolecular biologyActinsKelch proteinSubcellular FractionSettore BIO/18 - GeneticaGene Expression RegulationCytoplasmPhosphopyruvate Hydratasebiology.proteinHeLa CellsTranscription FactorsBiochimica et Biophysica Acta (BBA) - Molecular Cell Research
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A method for genome-wide analysis of DNA helical tension by means of psoralen-DNA photobinding

2010

The helical tension of chromosomal DNA is one of the epigenetic landmarks most difficult to examine experimentally. The occurrence of DNA crosslinks mediated by psoralen photobinding (PB) stands as the only suitable probe for assessing this problem. PB is affected by chromatin structure when is done to saturation; but it is mainly determined by DNA helical tension when it is done to very low hit conditions. Hence, we developed a method for genome-wide analysis of DNA helical tension based on PB. We adjusted in vitro PB conditions that discern DNA helical tension and applied them to Saccharomyces cerevisiae cells. We selected the in vivo cross-linked DNA sequences and identified them on DNA …

Transcription GeneticUltraviolet RaysSaccharomyces cerevisiaeMutantADNSaccharomyces cerevisiaeBiologyDNA sequencingGenètica molecularchemistry.chemical_compoundGeneticsTrioxsalenDNA FungalOligonucleotide Array Sequence AnalysisProbabilityTopoisomeraseChromosomeDNAGenomicsbiology.organism_classificationMolecular biologyChromatinNucleosomesChromatinDNA-Binding ProteinsGenòmicaCross-Linking ReagentschemistryNaked DNAbiology.proteinBiophysicsNucleic Acid ConformationMethods OnlineChromosomes FungalDNA TopoisomerasesDNA
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NFAT transcription factors control HIV-1 expression through a binding site downstream of TAR region.

2004

NFAT factors control HIV-1 transcription. We show here that, in addition to binding to two NF-kappaB/NFAT sites within the U3 HIV LTR, NFATc1 and NFATc2 bind to an NFAT site within the LTR's U5 region. Mutations in this site which abolish NFAT binding reduce the ability of NFATs to transactivate LTR-mediated transcription. Mutations in all three NFAT sites strongly interfered with LTR induction, but affected moderately the stimulatory effect of Tat.

Transcription GeneticvirusesImmunologyTransfectionJurkat cellsJurkat CellsTranscription (biology)Immunology and AllergyHumansNuclear proteinBinding siteTranscription factorHIV Long Terminal RepeatBinding SitesNFATC Transcription FactorsChemistryNuclear ProteinsNFATHematologyU937 CellsNFATC Transcription FactorsMolecular biologyDNA-Binding Proteinscardiovascular systemHIV-1HIV Long Terminal RepeatTranscription FactorsImmunobiology
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The relative role of the T-domain and flanking sequences for developmental control and transcriptional regulation in protein chimeras of Drosophila O…

2004

optomotor-blind (omb) and optomotor-blind related-1 (org-1) encode T-domain DNA binding proteins in Drosophila. Members of this family of transcription factors play widely varying roles during early development and organogenesis in both vertebrates and invertebrates. Functional specificity differs in spite of similar DNA binding preferences of all family members. Using a series of domain swap chimeras, in which different parts of OMB and ORG-1 were mutually exchanged, we investigated the relevance of individual domains in vitro and in vivo. In cell culture transfection assays, ORG-1 was a strong transcriptional activator, whereas OMB appeared neutral. The main transcriptional activation fun…

Transcriptional ActivationEmbryologyTranscription GeneticNerve Tissue ProteinsBiologyEyeDNA-binding proteinChimera (genetics)Transcriptional regulationAnimalsDrosophila ProteinsTransgenesCloning MolecularTranscription factorPsychological repressionGeneticsChimeraGene Transfer TechniquesGene Expression Regulation DevelopmentalProtein Structure TertiaryT-boxEye developmentMicroscopy Electron ScanningDrosophilaT-Box Domain ProteinsDrosophila ProteinDevelopmental BiologyMechanisms of Development
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Role of hepatocyte nuclear factor 3γ in the expression of human CYP2C genes

2004

Hepatocyte nuclear factor 3 gamma (HNF-3 gamma) is an important transcription factor for the maintenance of specific liver functions. However, its relevance in the expression of human cytochrome P450 (CYP) genes has not yet been explored. Several HNF3 putative binding sites can be identified in human CYP2C 5'-flanking regions. Gene reporter experiments with proximal promoters revealed that HNF-3 gamma transactivated CYP2C8, CYP2C9, and CYP2C19 (25-, 4-, and 4-fold, respectively), but it did not transactivate CYP2C18. However, overexpression of HNF-3 gamma in hepatoma cells by means of a recombinant adenovirus induced CYP2C9, CYP2C18, and CYP2C19 mRNA (4.5-, 20-, and 50-fold, respectively) b…

Transcriptional ActivationRecombinant Fusion ProteinsGenetic VectorsBiophysicsBiologyHydroxamic AcidsTransfectionBiochemistryGene Expression Regulation EnzymologicAdenoviridaeCytochrome P-450 Enzyme SystemSp3 transcription factorCell Line TumormedicineHumansRNA MessengerEnzyme InhibitorsLuciferasesPromoter Regions GeneticMolecular BiologyTranscription factorBinding SitesNuclear ProteinsPromoterMolecular biologyDNA-Binding ProteinsHistone Deacetylase InhibitorsHepatocyte nuclear factorsTrichostatin AHepatocyte nuclear factor 4Hepatocyte nuclear factor 4 alphaHepatocytesFOXA2Transcription Initiation SiteHepatocyte Nuclear Factor 3-gammaHeLa CellsTranscription Factorsmedicine.drugArchives of Biochemistry and Biophysics
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The yeast Aft1 transcription factor activates ribonucleotide reductase catalytic subunit RNR1 in response to iron deficiency

2020

Eukaryotic ribonucleotide reductases are iron-dependent enzymes that catalyze the rate-limiting step in the de novo synthesis of deoxyribonucleotides. Multiple mechanisms regulate the activity of ribonucleotide reductases in response to genotoxic stresses and iron deficiency. Upon iron starvation, the Saccharomyces cerevisiae Aft1 transcription factor specifically binds to iron-responsive cis elements within the promoter of a group of genes, known as the iron regulon, activating their transcription. Members of the iron regulon participate in iron acquisition, mobilization and recycling, and trigger a genome-wide metabolic remodeling of iron-dependent pathways. Here, we describe a mechanism …

Transcriptional ActivationRibonucleotideSaccharomyces cerevisiae ProteinsProtein subunitIronSaccharomyces cerevisiaeDeoxyribonucleotidesBiophysicsSaccharomyces cerevisiaeResponse ElementsBiochemistry03 medical and health sciencesStructural BiologyTranscription (biology)Gene Expression Regulation FungalRibonucleotide ReductasesGeneticsMolecular BiologyTranscription factorRibonucleotide reductase030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryIron deficiency030302 biochemistry & molecular biologyHigh Mobility Group ProteinsIron Deficienciesbiology.organism_classificationCell biologyDNA-Binding ProteinsRibonucleotide reductaseRegulonEnzymeYeast/TranscriptionProtein BindingTranscription Factors
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Yeast karyopherin Kap95 is required for cell cycle progression at Start

2010

Abstract Background The control of the subcellular localization of cell cycle regulators has emerged as a crucial mechanism in cell division regulation. The active transport of proteins between the nucleus and the cytoplasm is mediated by the transport receptors of the β-karyopherin family. In this work we characterized the terminal phenotype of a mutant strain in β-karyopherin Kap95, a component of the classical nuclear import pathway. Results When KAP95 was inactivated, most cells arrested at the G2/M phase of the cell cycle, which is in agreement with the results observed in mutants in the other components of this pathway. However, a number of cells accumulate at G1, suggesting a novel r…

Transcriptional ActivationSaccharomyces cerevisiae ProteinsNuclear Localization SignalsActive Transport Cell NucleusSaccharomyces cerevisiaeImportinBiologylcsh:QH573-671Transcription factorCells CulturedKaryopherinCell Nucleuschemistry.chemical_classificationlcsh:CytologyCell CycleCell BiologyCell cyclebeta KaryopherinsSubcellular localizationCell biologyDNA-Binding ProteinschemistryCytoplasmMutationTranscription Initiation SiteNuclear transportNuclear localization sequenceProtein BindingTranscription FactorsResearch ArticleBMC Cell Biology
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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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