Search results for "Small Nuclear"

showing 8 items of 18 documents

Evidence for involvement of a nuclear envelope-associated RNA helicase activity in nucleocytoplasmic RNA transport

1990

It seems well established that translocation of at least some mRNAs through the nuclear pore is (1) an energy-dependent process, and (2) dependent on the presence of the poly(A) segment attached to most mRNA species. We describe that RNA helicase (RNA duplex unwindase) activity is present in a nuclear envelope (NE) preparation, which also appears to be involved in nucleocytoplasmic RNA transport. This activity unwinds RNA: RNA hybrids. The helicase has a pH optimum of 7.5 and a temperature optimum of 30 degrees C. Applying the sealed NE vesicle system, it was shown that duplex RNA species are readily released from the vesicles in an unidirectional manner, in contrast to single-stranded RNA,…

PhysiologyClinical BiochemistryRNARNA-dependent RNA polymeraseRNA transportCell BiologyBiologyNon-coding RNARNA Helicase ABiochemistryRNA polymerase IBiophysicsDegradosomeSmall nuclear RNAJournal of Cellular Physiology
researchProduct

BASE-SPECIFIC RIBONUCLEASES POTENTIALLY INVOLVED IN HETEROGENEOUS NUCLEAR-RNA PROCESSING AND POLY(A) METABOLISM

1984

Abstract Polyadenylation and splicing of heterogeneous nuclear RNA, two crucial steps in mRNA processing, are apparently enzymically mediated processes. This contribution summarizes the properties and the presumed functions of the known poly(A) catabolic enzymes (endoribonuclease IV and V, 2′,3′-exoribonuclease) as well as those of the pyrimidine-specific endoribonucleases associated with snRNP—hnRNP complexes (endoribonuclease VII, acidic p I 4.1 endoribonuclease and poly(U)-specific U1 snRNP-nuclease).

Poly UPolyadenylationRNA SplicingsnRNPEndoribonucleaseBiophysicsPolyadenylationSplicingenvironment and public healthBiochemistryRibonucleaseRibonucleasesEndoribonucleasesPoly(A)+ mRNAStructural BiologyGeneticsAnimalssnRNPRNA MessengerRibonucleaseMolecular Biologychemistry.chemical_classificationMessenger RNABase SequencebiologyCell BiologyRibonucleoproteins Small NuclearhnRNA processingEnzymeRibonucleoproteinschemistryBiochemistryRNA splicingbiology.proteinNucleic Acid ConformationRNA Heterogeneous NuclearPoly A
researchProduct

Interaction of 68–kDa TAR RNA-binding protein and other cellular proteins with rpion protein-RNA stem-loop

1995

The RNA stem-loop structure of the trans-activating region TAR sequence of human immunodeficiency virus-1 mRNA is the binding site for a number of host cell proteins. A virtually identical set of proteins from HeLa nuclear extracts was found to bind to the predicted RNA hairpin element of prion protein (PrP) mRNA, as demonstrated in UV cross-linking/RNase protection and Northwestern assays. We show that the cellular TAR loop-binding protein, p68, is among those proteins which associate with PrP RNA. Competition experiments with various TAR RNA mutants revealed that binding of partially purified p68 to PrP RNA stem-loop occurs sequence-specifically. The 100-kDa 2-5A synthetase which is invol…

PrionsBlotting WesternMolecular Sequence DataRNA-dependent RNA polymeraseReceptors Cell SurfaceRNA-binding proteinBiologyBinding CompetitiveCellular and Molecular NeuroscienceVirology2'5'-Oligoadenylate SynthetaseHumansLymphocytesHIV Long Terminal RepeatBase SequenceRNA-Binding ProteinsRNABlotting NorthernNon-coding RNAMolecular biologyRNA silencingNeurologyMutagenesisRNA editingeIF4ANucleic Acid ConformationNeurology (clinical)Small nuclear RNAHeLa CellsJournal of Neurovirology
researchProduct

SANS (USH1G) regulates pre-mRNA splicing by mediating the intra-nuclear transfer of tri-snRNP complexes

2021

Abstract Splicing is catalyzed by the spliceosome, a compositionally dynamic complex assembled stepwise on pre-mRNA. We reveal links between splicing machinery components and the intrinsically disordered ciliopathy protein SANS. Pathogenic mutations in SANS/USH1G lead to Usher syndrome—the most common cause of deaf-blindness. Previously, SANS was shown to function only in the cytosol and primary cilia. Here, we have uncovered molecular links between SANS and pre-mRNA splicing catalyzed by the spliceosome in the nucleus. We show that SANS is found in Cajal bodies and nuclear speckles, where it interacts with components of spliceosomal sub-complexes such as SF3B1 and the large splicing cofact…

ProteomicsAcademicSubjects/SCI00010Ribonucleoprotein U4-U6 Small NuclearSF3B1 GeneMass Spectrometry0302 clinical medicineRNA Small NuclearRNA PrecursorsIn Situ Hybridization FluorescenceRibonucleoprotein0303 health sciencesChemistryRibonucleoproteins Small NuclearImmunohistochemistryCell biologyDNA-Binding Proteinsmedicine.anatomical_structureGene Knockdown TechniquesRNA splicingRNA Splicing FactorsUsher SyndromesSpliceosomeCoiled BodiesNerve Tissue ProteinsBiologyMinor Histocompatibility Antigens03 medical and health sciencesMicroscopy Electron TransmissionRNA and RNA-protein complexesGeneticsmedicineHumanssnRNPEye ProteinsGeneCell Proliferation030304 developmental biologyCell NucleusRNAmedicine.diseasePhosphoproteinsCiliopathyAlternative SplicingCell nucleusHEK293 CellsCajal bodyCytoplasmSpliceosomesNucleus030217 neurology & neurosurgeryTranscription FactorsNucleic Acids Research
researchProduct

Pseudouridine: Still mysterious, but never a fake (uridine)!

2014

International audience; Pseudouridine () is the most abundant of >150 nucleoside modifications in RNA. Although was discovered as the first modified nucleoside more than half a century ago, neither the enzymatic mechanism of its formation, nor the function of this modification are fully elucidated. We present the consistent picture of synthases, their substrates and their substrate positions in model organisms of all domains of life as it has emerged to date and point out the challenges that remain concerning higher eukaryotes and the elucidation of the enzymatic mechanism.

RNA MitochondrialSaccharomyces cerevisiaeReviewBiologyModified nucleosidesPseudouridine03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA modificationEscherichia coliHumansRNA Processing Post-Transcriptional[SDV.BBM.BC]Life Sciences [q-bio]/Biochemistry Molecular Biology/Biochemistry [q-bio.BM]Intramolecular TransferasesUridineMolecular Biology030304 developmental biology0303 health sciencesRNACell BiologyRNA Transfer Amino Acid-SpecificRibonucleoproteins Small NuclearUridineIsoenzymeschemistryBiochemistryRNA Ribosomal030220 oncology & carcinogenesisTransfer RNANucleic Acid ConformationRNARibosomesNucleosidePseudouridineSmall nuclear RNA[SDV.MHEP]Life Sciences [q-bio]/Human health and pathologyRNA Guide Kinetoplastida
researchProduct

Rtp1p Is a Karyopherin-Like Protein Required for RNA Polymerase II Biogenesis

2013

The assembly and nuclear transport of RNA polymerase II (RNA pol II) are processes that require the participation of many auxiliary factors. In a yeast genetic screen, we identified a previously uncharacterized gene, YMR185w (renamed RTP1), which encodes a protein required for the nuclear import of RNA pol II. Using protein affinity purification coupled to mass spectrometry, we identified interactions between Rtp1p and members of the R2TP complex. Rtp1p also interacts, to a different extent, with several RNA pol II subunits. The pattern of interactions is compatible with a role for Rtp1p as an assembly factor that participates in the formation of the Rpb2/Rpb3 subassembly complex and its bi…

Saccharomyces cerevisiae ProteinsActive Transport Cell NucleusRNA polymerase IISaccharomyces cerevisiaeKaryopherinsBiologyGene Expression Regulation FungalTranscriptional regulationRNA polymerase IProtein Interaction MapsMolecular BiologyRNA polymerase II holoenzymeR2TP complexGeneticsNuclear cap-binding protein complexArticlesCell BiologyPhosphoproteinsUp-RegulationCell biologyNuclear Pore Complex Proteinsbiology.proteinRNA Polymerase IITranscription factor II DCarrier ProteinsGene DeletionSmall nuclear RNATranscription Factors
researchProduct

MODOMICS: a database of RNA modification pathways—2013 update

2012

MODOMICS is a database of RNA modifications that provides comprehensive information concerning the chemical structures of modified ribonucleosides, their biosynthetic pathways, RNA-modifying enzymes and location of modified residues in RNA sequences. In the current database version, accessible at http://modomics.genesilico.pl, we included new features: a census of human and yeast snoRNAs involved in RNA-guided RNA modification, a new section covering the 5′-end capping process, and a catalogue of ‘building blocks’ for chemical synthesis of a large variety of modified nucleosides. The MODOMICS collections of RNA modifications, RNA-modifying enzymes and modified RNAs have been also updated. A…

TRNA modificationSequence analysisBiologycomputer.software_genre03 medical and health sciences0302 clinical medicineRNA Small NuclearEpitranscriptomicsGeneticsHumansRNA Small NucleolarRNA Processing Post-TranscriptionalSmall nucleolar RNA030304 developmental biologyGeneticsInternet0303 health sciencesDatabaseSequence Analysis RNAMRNA modificationRNAArticlesRibosomal RNAEnzymes3. Good healthTransfer RNARNADatabases Nucleic Acidcomputer030217 neurology & neurosurgeryNucleic Acids Research
researchProduct

Chromatin-dependent regulation of RNA polymerases II and III activity throughout the transcription cycle

2015

The particular behaviour of eukaryotic RNA polymerases along different gene regions and amongst distinct gene functional groups is not totally understood. To cast light onto the alternative active or backtracking states of RNA polymerase II, we have quantitatively mapped active RNA polymerases at a high resolution following a new biotin-based genomic run-on (BioGRO) technique. Compared with conventional profiling with chromatin immunoprecipitation, the analysis of the BioGRO profiles in Saccharomyces cerevisiae shows that RNA polymerase II has unique activity profiles at both gene ends, which are highly dependent on positioned nucleosomes. This is the first demonstration of the in vivo infl…

Transcription factoriesSaccharomyces cerevisiae ProteinsTranscription Elongation GeneticTranscription GeneticRNA polymerase II28Saccharomyces cerevisiaeBiology03 medical and health scienceschemistry.chemical_compoundTranscripció genèticaRNA polymeraseGeneticsRNA polymerase IRNA polymerase II holoenzyme9030304 developmental biologyGenetics0303 health sciencesGeneral transcription factorGene regulation Chromatin and Epigenetics030302 biochemistry & molecular biologyRNA Polymerase IIIGenomicsNucleosomesCell biologychemistryTranscription Termination Geneticbiology.proteinRNARNA Polymerase IIGenome FungalTranscription factor II DSmall nuclear RNA
researchProduct