Search results for "Cell Nucleus"

showing 10 items of 379 documents

Enhancer blocking activity located near the 3′ end of the sea urchin early H2A histone gene

1997

The sea urchin early histone repeating unit contains one copy of each of the five histone genes whose coordinate expression during development is regulated by gene-specific elements. To learn how within the histone repeating unit a gene-specific activator can be prevented to communicate with the heterologous promoters, we searched for domain boundaries by using the enhancer blocking assay. We focused on the region near the 3′ end of the H2A gene where stage-specific nuclease cleavage sites appear upon silencing of the early histone genes. We demonstrated that a DNA fragment of 265 bp in length, defined as sns (for silencing nucleoprotein structure), blocked the enhancer activity of the H2A…

Chloramphenicol O-AcetyltransferaseMaleSea urchinEmbryo Nonmammaliananimal structuresRecombinant Fusion ProteinsMolecular Sequence DataEnhancer RNAsSettore BIO/11 - Biologia MolecolareHistonesChloramphenicol acetyltransferaseAnimalsHumansEnhancer trapCoding regionAmino Acid SequencePromoter Regions GeneticEnhancerOvumRepetitive Sequences Nucleic AcidCell NucleusBase CompositionMultidisciplinaryBase SequencebiologyActivator (genetics)Histone genesPromoterGastrulaBiological SciencesSpermatozoaMolecular biologyEnhancer Elements GeneticNucleoproteinsHistoneSea UrchinsSettore BIO/03 - Botanica Ambientale E Applicatabiology.proteinFemaleEnhancer blocking activityHeLa Cells
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Chlamydomonas reinhardtii in the landscape of pigments.

2004

▪ Abstract  This review focuses on the biosynthesis of pigments in the unicellular alga Chlamydomonas reinhardtii and their physiological and regulatory functions in the context of information gathered from studies of other photosynthetic organisms. C. reinhardtii is serving as an important model organism for studies of photosynthesis and the pigments associated with the photosynthetic apparatus. Despite extensive information pertaining to the biosynthetic pathways critical for making chlorophylls and carotenoids, we are just beginning to understand the control of these pathways, the coordination between pigment and apoprotein synthesis, and the interactions between the activities of these…

ChlorophyllRhodopsinNuclear geneChloroplastsved/biology.organism_classification_rank.speciesLight-Harvesting Protein ComplexesProtozoan ProteinsChlamydomonas reinhardtiiPhotosynthesisModels Biologicalchemistry.chemical_compoundHemiterpenesLycopeneBiosynthesisIsomerismPentanesBotanyGeneticsButadienesAnimalsPhotosynthesisModel organismCarotenoidPlant Proteinschemistry.chemical_classificationCell Nucleusbiologyved/biologyPigments Biologicalbiology.organism_classificationCarotenoidsChloroplastOxygenCytochrome b6f ComplexchemistryBiochemistryXanthophyllPhotoreceptor Cells InvertebrateChlamydomonas reinhardtiiAnnual review of genetics
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ORGANIZATION OF HIGHER-LEVEL CHROMATIN STRUCTURES (CHROMOMERE, CHROMONEMA AND CHROMATIN BLOCK) EXAMINED USING VISIBLE LIGHT-INDUCED CHROMATIN PHOTO-S…

2002

The method of chromatin photo-stabilization by the action of visible light in the presence of ethidium bromide was used for investigation of higher-level chromatin structures in isolated nuclei. As a model we used rat hepatocyte nuclei isolated in buffers which stabilized or destabilized nuclear matrix. Several higher-level chromatin structures were visualized: 100 nm globules—chromomeres, chains of chromomeres—chromonemata, aggregates of chromomeres—blocks of condensed chromatin. All these structures were completely destroyed by 2 M NaCl extraction independent of the matrix state, and DNA was extruded from the residual nuclei (nuclear matrices) into a halo. These results show that nuclear …

ChromomereLightPhotochemistrySolenoid (DNA)BuffersBiologyRadiation Dosagechemistry.chemical_compoundMicroscopy Electron TransmissionNuclear Matrix-Associated ProteinsEthidiumAnimalsNucleoidChromatin structure remodeling (RSC) complexInterphaseCell NucleusCell BiologyGeneral MedicineNuclear matrixMolecular biologyChromatinProtein Structure TertiaryRatsChromatinDNA-Binding ProteinschemistryHepatocytesBiophysicsbiology.proteinInterphaseDNASubcellular FractionsCell Biology International
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Reorganization of Nuclear Domain 10 Induced by Papillomavirus Capsid Protein L2

2002

AbstractNuclear domains (ND) 10 are associated with proteins implicated in transcriptional regulation, growth suppression, and apoptosis. We now show that the minor capsid protein L2 of human papillomavirus (HPV) type 33 induces a reorganization of ND10-associated proteins. Whereas the promyelocytic leukemia protein, the major structural component of ND10, was unaffected by L2, Sp100 was released from ND10 upon L2 expression. The total cellular amount of Sp100, but not of Sp100 mRNA, decreased significantly, suggesting degradation of Sp100. Proteasome inhibitors induced the dispersal of Sp100 and inhibited the nuclear translocation of L2. In contrast to Sp100, Daxx was recruited to ND10 by …

Co-Repressor ProteinsImmunoprecipitationFluorescent Antibody TechniqueVaccinia virusPromyelocytic Leukemia ProteinAutoantigenspapillomavirusCell LinePromyelocytic leukemia proteinCapsidDeath-associated protein 6DaxxVirologyHumansSp100RNA MessengerAdaptor Proteins Signal TransducingCell NucleusRecombination GeneticbiologyTumor Suppressor ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsND10Signal transducing adaptor proteinAntigens NuclearOncogene Proteins ViralL2biochemical phenomena metabolism and nutritionBlotting NorthernMolecular biologyNeoplasm ProteinsTransport proteinCell biologyProtein TransportProteasomeCapsidbiology.proteinRNACapsid ProteinsFemaleCarrier ProteinsCo-Repressor ProteinsMolecular ChaperonesTranscription FactorsVirology
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Heat shock and Cd2+ exposure regulate PML and Daxx release from ND10 by independent mechanisms that modify the induction of heat-shock proteins 70 an…

2003

Nuclear domains called ND10 or PML bodies might function as nuclear depots by recruiting or releasing certain proteins. Although recruitment of proteins through interferon-induced upregulation and SUMO-1 modification level of PML had been defined, it is not known whether release of proteins is regulated and has physiological consequences. Exposure to sublethal environmental stress revealed a sequential release of ND10-associated proteins. Upon heat shock Daxx and Sp100 were released but PML remained, whereas exposure to subtoxic concentrations of CdCl2 induced the release of ND10-associated proteins, including PML, with Sp100 remaining in a few sites. In both cases,recovery times were simil…

Co-Repressor ProteinsMAP Kinase Signaling SystemMacromolecular SubstancesSUMO-1 ProteinPromyelocytic Leukemia ProteinMicePromyelocytic leukemia proteinDeath-associated protein 6Stress PhysiologicalHeat shock proteinEndopeptidasesAnimalsHSP70 Heat-Shock ProteinsEnzyme InhibitorsHeat shockTranscription factorCells CulturedHeat-Shock ProteinsbiologyTumor Suppressor ProteinsIntracellular Signaling Peptides and ProteinsNuclear ProteinsCell BiologyCell Nucleus StructuresNeoplasm ProteinsCell biologyHsp70Cysteine EndopeptidasesEukaryotic CellsGene Expression RegulationImmunologybiology.proteinSignal transductionCarrier ProteinsCo-Repressor ProteinsHeat-Shock ResponseCadmiumMolecular ChaperonesTranscription FactorsJournal of Cell Science
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Dynamics and interactions of parvoviral NS1 protein in the nucleus

2007

Summary Nuclear positioning and dynamic interactions of viral proteins with nuclear substructures play essen- tial roles during infection with DNA viruses. Visual- ization of the intranuclear interactions and motility of the parvovirus replication protein (NS1) in living cells gives insight into specific parvovirus protein- cellular structure interactions. Confocal analysis of highly synchronized infected Norden Laboratory Feline Kidney cells showed accumulation of nuclear NS1 in discrete interchromosomal foci. NS1 fused with enhanced yellow fluorescence protein (NS1- EYFP) provided a marker in live cells for dynamics of NS1 traced by photobleaching techniques. Fluo- rescence Recovery after…

ConfocalvirusesImmunologyMotilityViral Nonstructural ProteinsBiologyVirus ReplicationMicrobiologyCell LineParvoviruschemistry.chemical_compoundBacterial ProteinsVirologymedicineAnimalsFluorescence loss in photobleachingCell NucleusPhotobleachingParvovirusvirus diseasesbiochemical phenomena metabolism and nutritionbiology.organism_classificationMolecular biologyFluorescencePhotobleachingCell biologyLuminescent Proteinsmedicine.anatomical_structurechemistryCatsNucleusDNACellular Microbiology
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The Origin of Isolated Populations of the Mountain Weevil, Liparus glabrirostris—The Flagship Species for Riparian Habitats

2020

AbstractLiparus glabrirostris is one of the largest European weevils, and it has been recently proposed as the flagship species for threatened riparian habitats in the mountains. For effective conservation of its populations (and associated habitats), it is crucial to understand its history, contemporary distribution, genetic diversity and predict changes in the range, including its highly isolated populations on the Baltic coast. Here, we examined numerous populations of L. glabrirostris across almost the entire species range using phylogeography and species niche modeling (SNM) approaches. Analyses of mtDNA and nucDNA markers revealed the existence of 2 major mitochondrial lineages genera…

Conservation geneticsGenetic MarkersConservation of Natural ResourcesRange (biology)Species distributionBiologyphylogeographyspecies distribution modelingDNA MitochondrialCurculionidaeGeneticsFlagship speciesAnimalsMolecular BiologyGenetics (clinical)EcosystemRiparian zoneCell Nucleusgeographygeography.geographical_feature_categoryEcologyEnvironmental niche modellingEuropeColeopteraPhylogeographyGenetics PopulationRefugiumconservation geneticsThreatened speciesWeevilsBiotechnologyJournal of Heredity
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Aryl hydrocarbon receptor activation by cAMP vs. dioxin: divergent signaling pathways.

2005

Even before the first vertebrates appeared on our planet, the aryl hydrocarbon receptor ( AHR ) gene was present to carry out one or more critical life functions. The vertebrate AHR then evolved to take on functions of detecting and responding to certain classes of environmental toxicants. These environmental pollutants include polycyclic aromatic hydrocarbons (e.g., benzo[ a ]pyrene), polyhalogenated hydrocarbons, dibenzofurans, and the most potent small-molecular-weight toxicant known, 2,3,7,8-tetrachlorodibenzo- p -dioxin (TCDD or dioxin). After binding of these ligands, the activated AHR translocates rapidly from the cytosol to the nucleus, where it forms a heterodimer with aryl hydroc…

Conservation of Natural ResourcesAryl hydrocarbon receptor nuclear translocatorPolychlorinated DibenzodioxinsTime FactorsTranscription GeneticGenetic VectorsGreen Fluorescent ProteinsImmunoblottingActive Transport Cell NucleusEnvironmentDioxinsLigandschemistry.chemical_compoundMiceCytosolGenes ReporterCell Line TumorCyclic AMPAnimalsImmunoprecipitationReceptorFluorescent Antibody Technique IndirectCell NucleusMultidisciplinarybiologyChemistryColforsinEndogenous mediatorrespiratory systemBiological SciencesAryl hydrocarbon receptorCyclic AMP-Dependent Protein KinasesCytosolProtein TransportBiochemistryBucladesineMicroscopy FluorescenceReceptors Aryl HydrocarbonSecond messenger systembiology.proteinProstaglandinsEnvironmental PollutantsSignal transductionDimerizationToxicantPlasmidsProtein BindingSignal TransductionProceedings of the National Academy of Sciences of the United States of America
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Calmodulin binds to p21(Cip1) and is involved in the regulation of its nuclear localization.

1999

p21(Cip1), first described as an inhibitor of cyclin-dependent kinases, has recently been shown to have a function in the formation of cyclin D-Cdk4 complexes and in their nuclear translocation. The dual behavior of p21(Cip1) may be due to its association with other proteins. Different evidence presented here indicate an in vitro and in vivo interaction of p21(Cip1) with calmodulin: 1) purified p21(Cip1) is able to bind to calmodulin-Sepharose in a Ca(2+)-dependent manner, and this binding is inhibited by the calmodulin-binding domain of calmodulin-dependent kinase II; 2) both molecules coimmunoprecipitate when extracted from cellular lysates; and 3) colocalization of calmodulin and p21(Cip…

Cyclin-Dependent Kinase Inhibitor p21CalmodulinMolecular Sequence DataBiologyBiochemistryCell LineCalmodulinIn vivoCyclinsProto-Oncogene ProteinsmedicineAnimalsCyclin D1Amino Acid SequencePhosphorylationMolecular BiologyCyclinCell NucleusSulfonamidesKinaseColocalizationCyclin-Dependent Kinase 4Cell BiologyImmunogold labellingPrecipitin TestsCyclin-Dependent KinasesCell biologyRatsEnzyme ActivationCell nucleusMicroscopy Electronmedicine.anatomical_structurebiology.proteinNuclear localization sequenceProtein BindingThe Journal of biological chemistry
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Myc Promoter-Binding Protein-1 (MBP-1) Is a Novel Potential Prognostic Marker in Invasive Ductal Breast Carcinoma

2010

BackgroundAlpha-enolase is a glycolytic enzyme that catalyses the formation of phosphoenolpyruvate in the cell cytoplasm. α-Enolase and the predominantly nuclear Myc promoter-binding protein-1 (MBP-1) originate from a single gene through the alternative use of translational starting sites. MBP-1 binds to the P2 c-myc promoter and competes with TATA-box binding protein (TBP) to suppress gene transcription. Although several studies have shown an antiproliferative effect of MBP-1 overexpression on several human cancer cells, to date detailed observations of α-enolase and MBP-1 relative expression in primary tumors versus normal tissues and their correlation with clinicopathological features ha…

CytoplasmAlpha-enolasePROGRESSIONAged 80 and overRegulation of gene expressionMultidisciplinaryQRGenetics and Genomics/Gene ExpressionMiddle AgedPrognosisPathology/Molecular PathologyNUDE-MICETransport proteinCarcinoma DuctalDNA-Binding ProteinsGene Expression Regulation NeoplasticProtein Transportmedicine.anatomical_structureGLYCOLYTIC ENZYMEOncology/Breast CancerMedicineCELL LUNG-CANCER; ALPHA-ENOLASE; PROTEOMIC ANALYSIS; GLYCOLYTIC ENZYME; NUDE-MICE; GENE; IDENTIFICATION; PROGRESSION; EXPRESSION; METASTASESFemalePROTEOMIC ANALYSISEnolase MBP-1 Breast cancer ImmunohistochemistryResearch ArticleAdultEXPRESSIONScienceCELL LUNG-CANCERBreast NeoplasmsBiologyDNA-binding proteinBiomarkers TumormedicineHumansNeoplasm InvasivenessGeneAgedCell NucleusIDENTIFICATIONBinding proteinALPHA-ENOLASEGENEMolecular biologySettore BIO/18 - GeneticaCell nucleusMETASTASESCytoplasmPhosphopyruvate Hydratasebiology.proteinPLoS ONE
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