Search results for "Nuclear proteins"

showing 10 items of 295 documents

Expression of the genetic suppressor element 24.2 (GSE24.2) decreases DNA damage and oxidative stress in X-linked dyskeratosis congenita cells.

2014

This is an open-access article distributed under the terms of the Creative Commons Attribution License.-- et al.

TelomeraseDNA repairDNA damagelcsh:MedicineCell Cycle ProteinsComputingMilieux_LEGALASPECTSOFCOMPUTINGBiologyTransfectionBioinformaticsmedicine.disease_causeBiochemistryDyskeratosis CongenitaDyskerinCell LineMiceHeterochromatinMolecular Cell BiologyMedicine and Health SciencesmedicineAnimalsHumanslcsh:ScienceMutationMultidisciplinarylcsh:RBiology and Life SciencesNuclear ProteinsCell BiologyHematologyGenetic TherapyTransfectionTelomeremedicine.diseaseTelomereCell biologyOxidative StressGene Expression Regulationlcsh:QPeptidesDyskeratosis congenitaResearch ArticleDNA DamagePLoS ONE
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Metazoan Circadian Rhythm: Toward an Understanding of a Light-Based Zeitgeber in Sponges

2013

In all eukaryotes, the 24-h periodicity in the environment contributed to the evolution of the molecular circadian clock. We studied some elements of a postulated circadian clock circuit in the lowest metazoans, the siliceous sponges. First, we identified in the demosponge Suberites domuncula the enzyme luciferase that generates photons. Then (most likely), the photons generated by luciferase are transmitted via the biosilica glass skeleton of the sponges and are finally harvested by cryptochrome in the same individual; hence, cryptochrome is acting as a photosensor. This information-transduction system, generation of light (luciferase), photon transmission (through the siliceous spicules),…

Time FactorsLightCircadian clockPlant Science03 medical and health sciencesDemospongeCryptochromeZeitgeberAnimalsLuciferasesGlycoproteins030304 developmental biologyRegulation of gene expression0303 health sciencesbiologyChemistry030302 biochemistry & molecular biologyNuclear Proteinsbiology.organism_classificationCircadian RhythmPoriferaCell biologyCryptochromesSuberites domunculaSpongeGene Expression RegulationGlucosyltransferasesAnimal Science and ZoologyExoribonuclease activitySignal TransductionTranscription Factors
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Transcriptional regulation of the stem cell leukemia gene by PU.1 and Elf-1.

1998

Abstract The SCL gene, also known astal-1, encodes a basic helix-loop-helix transcription factor that is pivotal for the normal development of all hematopoietic lineages. SCL is expressed in committed erythroid, mast, and megakaryocytic cells as well as in hematopoietic stem cells. Nothing is known about the regulation of SCL transcription in mast cells, and in other lineages GATA-1 is the only tissue-specific transcription factor recognized to regulate the SCL gene. We have therefore analyzed the molecular mechanisms underlyingSCL expression in mast cells. In this paper, we demonstrate that SCL promoter 1a was regulated by GATA-1 together with Sp1 and Sp3 in a manner similar to the situati…

Transcription GeneticDNA FootprintingBiologyBiochemistryCell LineMiceTranscription (biology)hemic and lymphatic diseasesProto-Oncogene ProteinsmedicineTranscriptional regulationBasic Helix-Loop-Helix Transcription FactorsAnimalsMast CellsPromoter Regions GeneticMolecular BiologyTranscription factorT-Cell Acute Lymphocytic Leukemia Protein 1DNA PrimersBase SequenceGATA2Nuclear ProteinsGATA1Cell BiologyMast cellMolecular biologyDNA-Binding ProteinsHaematopoiesismedicine.anatomical_structureGene Expression RegulationMutagenesis Site-DirectedTrans-ActivatorsStem cellTranscription FactorsThe Journal of biological chemistry
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Nuclear factors binding to the extensin promoter exhibit differential activity in carrot protoplasts and cells

1992

The expression of the cell wall protein extensin, a hydroxyproline-rich glycoprotein, is induced by several different stimuli, including wounding. The process of protoplast preparation mimics the wounding effect and results in the induction of extensin. Using transient expression in protoplasts we analyzed several deletions of the extensin promoter. We identified an important transcriptional regulatory element located between the two TATA boxes that characterize the extensin promoter. Other regulatory elements, located further upstream between -719 to -658, are necessary for maximum level of expression. Employing electrophoretic mobility shift assays and methylation interference experiments…

Transcription GeneticMolecular Sequence DataPlant ScienceBiologyDNA-binding proteinCell wallGene expressionGeneticsCloning MolecularPromoter Regions GeneticExtensinGlucuronidaseGlycoproteinsPlant ProteinsBinding SitesBase SequenceProtoplastsNuclear ProteinsDNAGeneral MedicineMethylationPlantsProtoplastMolecular biologyDNA-Binding ProteinsGene Expression RegulationRegulatory sequencebiology.proteinTrans-actingAgronomy and Crop SciencePlant Molecular Biology
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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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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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Sus1, a functional component of the SAGA histone acetylase complex and the nuclear pore-associated mRNA export machinery

2004

12 páginas, 7 figuras, 1 tabla. Material suplementario en: https://doi.org/10.1016/S0092-8674(03)01025-0. The SUS1 sequences have been deposited in GenBank with the accession number AY278445.

Transcriptional ActivationNucleocytoplasmic Transport ProteinsDNA ComplementarySaccharomyces cerevisiae ProteinsMolecular Sequence DataActive Transport Cell NucleusPorinsRNA polymerase IIBiologyGeneral Biochemistry Genetics and Molecular BiologyFungal ProteinsTranscription (biology)AcetyltransferasesGene Expression Regulation FungalYeastsGene expressionGenes RegulatorTranscriptional regulationAmino Acid SequenceRNA MessengerNuclear proteinPromoter Regions GeneticHistone AcetyltransferasesRegulation of gene expressionCell NucleusBase SequenceBiochemistry Genetics and Molecular Biology(all)Nuclear ProteinsRNA-Binding ProteinsMolecular biologyCell biologySAGA complexRibonucleoproteinsbiology.proteinNuclear PoreGenes LethalChromatin immunoprecipitation
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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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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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