Search results for "Ribonucleoprotein particle"

showing 9 items of 9 documents

FORMATION OF A SMALL RIBONUCLEOPROTEIN PARTICLE BETWEEN TAT PROTEIN AND TRANS-ACTING RESPONSE ELEMENT IN HUMAN IMMUNODEFICIENCY VIRUS-INFECTED CELLS

1991

The trans-acting response element (TAR) within the long terminal repeat of human immunodeficiency virus (HIV) is present in all 5' termini of HIV mRNAs and is recognized by the viral Tat protein. Now we describe that the 59-nucleotide-long TAR-RNA exists as a ribonucleoprotein particle in polysomal and heterogeneous nuclear RNP fractions of HIV-1-infected HeLa-T4+ cells. Applying an immunoprecipitation technique this Tat.TAR complex could be isolated from total cell extracts as well as from polysomal or heterogeneous nuclear RNP fractions. The chain length and the identity of the TAR-RNA were established by RNase protection assays while the Tat protein was confirmed by Western blotting tech…

chemistry.chemical_classificationMessenger RNAImmunoprecipitationvirusesResponse elementRibonucleoprotein particleCell BiologyBiologycomplex mixturesBiochemistryMolecular biologyLong terminal repeatchemistry.chemical_compoundchemistryotorhinolaryngologic diseasesNucleotideMolecular BiologyDNARibonucleoprotein
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ISWI ATP-dependent remodeling of nucleoplasmic ω-speckles in the brain of Drosophila melanogaster.

2017

Heterogeneous nuclear ribonucleoproteins (hnRNPs) belong to the RNA-binding proteins family. They are involved in processing heterogeneous nuclear RNAs (hnRNAs) into mature mRNAs. These proteins participate in every step of mRNA cycle, such as mRNA export, localization, translation, stability and alternative splicing. At least 14 major hnRNPs, which have structural and functional homologues in mammals, are expressed in Drosophila melanogaster. Until now, six of these hnRNPs are known to be nucleus-localized and associated with the long non-coding RNA (lncRNA) heat shock responsive ω (hsrω) in the omega speckle compartments (ω-speckles). The chromatin remodeler ISWI is the catalytic subunit …

0301 basic medicineTranscription GeneticBiologyHeterogeneous ribonucleoprotein particleHeterogeneous-Nuclear RibonucleoproteinsNuclear body03 medical and health scienceslncRNAAdenosine TriphosphateChromatin remodelersGene expressionGeneticsOmega speckleAnimalsMolecular BiologyGeneticsAdenosine TriphosphatasesCell NucleusAlternative splicingChromatin remodelers; hnRNPs; lncRNA; Nuclear body; Omega speckles; Molecular Biology; GeneticsRNABrainTranslation (biology)biology.organism_classificationChromatin Assembly and DisassemblyhnRNPsChromatinCell biology030104 developmental biologyDrosophila melanogasterGene Expression RegulationOmega specklesDrosophila melanogasterTranscription FactorsJournal of genetics and genomics = Yi chuan xue bao
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The ISWI chromatin remodeler organizes the hsrω ncRNA-containing omega speckle nuclear compartments.

2011

The complexity in composition and function of the eukaryotic nucleus is achieved through its organization in specialized nuclear compartments. The Drosophila chromatin remodeling ATPase ISWI plays evolutionarily conserved roles in chromatin organization. Interestingly, ISWI genetically interacts with the hsrω gene, encoding multiple non-coding RNAs (ncRNA) essential, among other functions, for the assembly and organization of the omega speckles. The nucleoplasmic omega speckles play important functions in RNA metabolism, in normal and stressed cells, by regulating availability of hnRNPs and some other RNA processing proteins. Chromatin remodelers, as well as nuclear speckles and their assoc…

MaleCancer ResearchRNA Untranslatedlcsh:QH426-470Gene ExpressionFluorescent Antibody TechniqueRNA-binding proteinBiologyEyeHeterogeneous ribonucleoprotein particleChromosomesHeterogeneous-Nuclear RibonucleoproteinsChromatin remodelingMolecular GeneticsGeneticsmedicineAnimalsDrosophila ProteinsOmega speckleBiologyMolecular BiologyTranscription factorAllelesGenetics (clinical)Ecology Evolution Behavior and SystematicsAdenosine TriphosphatasesCell NucleusGeneticsRNA-Binding ProteinsEpistasis GeneticChromatin Assembly and DisassemblyNon-coding RNAChromatinCell biologyCell nucleuslcsh:GeneticsPhenotypemedicine.anatomical_structureTandem Repeat SequencesChromatin remodeling non coding RNALarvaEpigeneticsDrosophilaRNA InterferenceResearch ArticleTranscription FactorsPLoS Genetics
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Proteome-Wide Characterization of the RNA-Binding Protein RALY-Interactome Using the in Vivo-Biotinylation-Pulldown-Quant (iBioPQ) Approach

2013

RALY is a member of the heterogeneous nuclear ribonucleoproteins, a family of RNA-binding proteins generally involved in many processes of mRNA metabolism. No quantitative proteomic analysis of RALY-containing ribonucleoparticles (RNPs) has been performed so far, and the biological role of RALY remains elusive. Here, we present a workflow for the characterization of RALY's interaction partners, termed iBioPQ, that involves in vivo biotinylation of biotin acceptor peptide (BAP)-fused protein in the presence of the prokaryotic biotin holoenzyme synthetase of BirA so that it can be purified using streptavidin-coated magnetic beads, circumventing the need for specific antibodies and providing e…

ProteomeRecombinant Fusion ProteinsMolecular Sequence DataBiotinRNA-binding proteinBiologyHeterogeneous ribonucleoprotein particleProteomicsPoly(A)-Binding Protein IBiochemistryInteractomeELAV-Like Protein 103 medical and health scienceschemistry.chemical_compound0302 clinical medicineNuclear Matrix-Associated ProteinsBiotinProtein Interaction MappingHumansCarbon-Nitrogen LigasesAmino Acid SequenceProtein Interaction MapsPeptide sequence030304 developmental biology0303 health sciencesEscherichia coli ProteinsHeterogeneous-Nuclear Ribonucleoprotein Group CRNA-Binding ProteinsGeneral ChemistryRepressor ProteinsHEK293 CellsELAV ProteinsGene Expression RegulationBiochemistrychemistryProtein Biosynthesis030220 oncology & carcinogenesisBiotinylationProteomeBiological AssayStreptavidinHeLa CellsProtein BindingJournal of Proteome Research
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Alteration of major vault protein in human glioblastoma and its relation with EGFR and PTEN status.

2014

Glioblastoma (GBM) is the most frequent and malignant primary brain tumor. Conventional therapy of surgical removal, radiation and chemotherapy is largely palliative. Major vault protein (MVP), the main component of the vault organelle has been associated with multidrug resistance by reducing cellular accumulation of chemotherapeutic agents. With regard to cancer, MVP has been shown to be overexpressed in drug resistance development and malignant progression. The aim of the present study was to evaluate the MVP gene dosage levels in 113 archival samples from GBM and its correlation with patients' survival and epidermal growth factor receptor (EGFR) and phosphatase and tensin homolog (PTEN) …

AdultMaleBiologyGene dosageStatistics NonparametricYoung AdultMajor vault proteinmedicinePTENTensinHumansEpidermal growth factor receptorMultiplex ligation-dependent probe amplificationAgedVault Ribonucleoprotein ParticlesPolysomyBrain NeoplasmsGeneral NeurosciencePTEN PhosphohydrolaseCancerMiddle Agedmedicine.diseaseErbB ReceptorsGene Expression Regulation NeoplasticMutationCancer researchbiology.proteinFemaleGlioblastomaChromosomes Human Pair 7Neuroscience
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Identification in the rat brain of a set of nuclear proteins interacting with H1° mRNA

2012

Synthesis of H1° histone, in the developing rat brain, is also regulated at post-transcriptional level. Regulation of RNA metabolism depends on a series of RNA-binding proteins (RBPs); therefore, we searched for H1° mRNA-interacting proteins. With this aim, we used in vitro transcribed, biotinylated H1° RNA as bait to isolate, by a chromatographic approach, proteins which interact with this mRNA, in the nuclei of brain cells. Abundant RBPs, such as heterogeneous nuclear ribonucleoprotein (hnRNP) K and hnRNP A1, and molecular chaperones (heat shock cognate 70, Hsc70) were identified by mass spectrometry. Western blot analysis also revealed the presence of cold shock domain-containing protein…

Heterogeneous nuclear ribonucleoproteinRNA-binding proteinRNA-binding proteinBiologyenvironment and public healthHeterogeneous-Nuclear RibonucleoproteinsMass SpectrometryHistonesSettore BIO/10 - BiochimicaAnimalsRNA MessengerNuclear proteinRats WistarSettore BIO/06 - Anatomia Comparata E CitologiaRibonucleoproteinMessenger RNAPIPPinGeneral NeuroscienceRibonucleoprotein particleHSC70 Heat-Shock ProteinsRNABrainCSD-C2Molecular biologyCell biologyRatsHistonebiology.proteinH1° mRNAPost-transcriptional gene regulation
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Proteomic analysis reveals a role for Bcl2-associated athanogene 3 and major vault protein in resistance to apoptosis in senescent cells by regulatin…

2014

Senescence is a prominent solid tumor response to therapy in which cells avoid apoptosis and instead enter into prolonged cell cycle arrest. We applied a quantitative proteomics screen to identify signals that lead to therapy-induced senescence and discovered that Bcl2-associated athanogene 3 (Bag3) is up-regulated after adriamycin treatment in MCF7 cells. Bag3 is a member of the BAG family of co-chaperones that interacts with Hsp70. Bag3 also regulates major cell-signaling pathways. Mass spectrometry analysis of the Bag3 Complex revealed a novel interaction between Bag3 and Major Vault Protein (MVP). Silencing of Bag3 or MVP shifts the cellular response to adriamycin to favor apoptosis. We…

SenescenceProteomicsCell cycle checkpointApoptosisBreast NeoplasmsBAG3BiochemistryAnalytical ChemistryMajor vault proteinCell Line TumorGene silencingHumansMolecular BiologyCellular SenescenceAdaptor Proteins Signal TransducingVault Ribonucleoprotein ParticlesMitogen-Activated Protein Kinase 1Antibiotics AntineoplasticMitogen-Activated Protein Kinase 3biologyResearchCell biologyApoptosisDoxorubicinbiology.proteinCancer researchSignal transductionApoptosis Regulatory ProteinsCell agingSignal TransductionMolecularcellular proteomics : MCP
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Activation of oligodendroglial Fyn kinase enhances translation of mRNAs transported in hnRNP A2-dependent RNA granules.

2008

Central nervous system myelination requires the synthesis of large amounts of myelin basic protein (MBP) at the axon–glia contact site. MBP messenger RNA (mRNA) is transported in RNA granules to oligodendroglial processes in a translationally silenced state. This process is regulated by the trans-acting factor heterogeneous nuclear ribonucleoprotein (hnRNP) A2 binding to the cis-acting A2 response element (A2RE). Release of this repression of MBP mRNA translation is thus essential for myelination. Mice deficient in the Src family tyrosine kinase Fyn are hypomyelinated and contain reduced levels of MBP. Here, we identify hnRNP A2 as a target of activated Fyn in oligodendrocytes. We show that…

Heterogeneous nuclear ribonucleoproteinCell Adhesion Molecules NeuronalRecombinant Fusion ProteinsBiologyHeterogeneous ribonucleoprotein particleCytoplasmic GranulesProto-Oncogene Proteins c-fynResponse Elementsenvironment and public healthRNA TransportCell LineMiceFYNContactinsGenes ReporterReportHeterogeneous-Nuclear Ribonucleoprotein Group A-BProtein biosynthesisAnimalsRNA MessengerPhosphorylationLuciferasesNeural Cell Adhesion MoleculesResearch ArticlesMessenger RNARNATranslation (biology)Cell BiologyMolecular biologyMyelin basic proteinEnzyme ActivationOligodendroglianervous systemProtein Biosynthesisbiology.proteinProtein BindingThe Journal of cell biology
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Loss of ISWI Function in Drosophila Nuclear Bodies Drives Cytoplasmic Redistribution of Drosophila TDP-43

2018

Over the past decade, evidence has identified a link between protein aggregation, RNA biology, and a subset of degenerative diseases. An important feature of these disorders is the cytoplasmic or nuclear aggregation of RNA-binding proteins (RBPs). Redistribution of RBPs, such as the human TAR DNA-binding 43 protein (TDP-43) from the nucleus to cytoplasmic inclusions is a pathological feature of several diseases. Indeed, sporadic and familial forms of amyotrophic lateral sclerosis (ALS) and fronto-temporal lobar degeneration share as hallmarks ubiquitin-positive inclusions. Recently, the wide spectrum of neurodegenerative diseases characterized by RBPs functions’ alteration and loss was coll…

0301 basic medicineCytoplasmCytoplasmic inclusionFluorescent Antibody TechniqueProtein aggregationHeterogeneous ribonucleoprotein particleHeterogeneous-Nuclear Ribonucleoproteinslcsh:Chemistry0302 clinical medicineDrosophila Proteinsneurodegenerative diseasesnuclear bodylcsh:QH301-705.5SpectroscopyGeneral MedicinehnRNPsComputer Science ApplicationsCell biologyChromatinTransport proteinDNA-Binding ProteinsProtein Transportmedicine.anatomical_structureDrosophilaDrosophila ProteinProtein BindingImitation SWIBiologyCatalysisArticleInorganic Chemistryomega speckles03 medical and health sciencesmedicineAnimalsPhysical and Theoretical ChemistryMolecular BiologyGenetic Association StudiesCell NucleusOrganic Chemistryta1182Chromatin Assembly and DisassemblyCell nucleus030104 developmental biologylcsh:Biology (General)lcsh:QD1-999gene expression<i>Drosophila</i>; nuclear body; omega speckles; dTDP-43; hnRNPs; omega speckles; neurodegenerative diseases; gene expression; gene regulationdTDP-43gene regulation030217 neurology & neurosurgeryInternational Journal of Molecular Sciences
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