Search results for "Endoribonuclease"

showing 9 items of 19 documents

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
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Influence of the xyloadenosine analogue of 2?,5?-oligoriboadenylate on poly(A)-specific, 2?,5?-oligoriboadenylate degrading 2?,3?-exoribonuclease and…

1984

The homogeneous poly(A)-specific 2′,3′-exoribonuclease from calf thymus gland, which cleaves both 3′,5′-and 2′,5′-linked oligoriboadenylates, does not degrade (xyloA2'p)2 xyloA, the xylofuranosyladenosine analogue of the 2-5A core. This oligonucleotide, which is supposed to enter intact cells rapidly, was found to possess an increased stability and an enhanced antiherpesvirus activity compared to the natural (A2'p)2A (Eppstein, D. A., Barnett, J. W., Marsh, Y. V., Gosselin, G. and Imbach, J.-L. (1983) Nature 302, 723–724). The poly(A) anabolic enzyme, poly(A) polymerase (Mn2+-dependent), from the same source, which is initiated by (A3'p)2A and its higher oligomers, does not accept 2–5A core…

PolyadenylationOligonucleotidesIn Vitro TechniquesOligomerchemistry.chemical_compoundExoribonucleaseEndoribonucleasesGeneticsAnimalsRNA MessengerMolecular BiologyPolymerasechemistry.chemical_classificationOligoribonucleotidesbiologyAdenine NucleotidesOligonucleotidePolynucleotide AdenylyltransferaseGeneral MedicineMolecular biologyPost-transcriptional modificationEnzymeRibonucleoproteinsBiochemistrychemistryExoribonucleasesbiology.proteinCattlePrimer (molecular biology)Poly AMolecular Biology Reports
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The mitochondrial genome of Schizosaccharomyces pombe. Stimulation of intra-chromosomal recombination in Escherichia coli by the gene product of the …

1991

The open reading frame of the first intron of the mitochondrial cox1 gene (cox1I1) was expressed in Escherichia coli. The putative intron-encoded protein stimulated the formation of intra-chromosomal lac +-recombinants about threefold. No stimulation was found when the reading frame was inserted in the opposite direction, or when it was interrupted by a deletion. The intronic open reading frame did not complement recA − or recB − mutants of E. coli. In S. pombe, elimination of this intron did not abolish homologous recombination in mitochondria. A possible role of the recombinase activity in yeast mitochondria will be discussed.

RNA SplicingGenes FungalMolecular Sequence DataSaccharomyces cerevisiaeBiologymedicine.disease_causeDNA MitochondrialElectron Transport Complex IVFungal ProteinsRecombinasesOpen Reading FramesSequence Homology Nucleic AcidEndoribonucleasesSchizosaccharomycesGeneticsmedicineRecombinaseEscherichia coliAmino Acid SequenceDNA FungalEscherichia coliRecBCDRecombination GeneticRecombinase activityBase SequenceIntegrasesIntronGeneral Medicinebiology.organism_classificationMolecular biologyNucleotidyltransferasesIntronsOpen reading frameSchizosaccharomyces pombeDNA NucleotidyltransferasesbacteriaHomologous recombination
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Alterations of Activities of Ribonucleases and Polyadenylate Polymerase in Synchronized Mouse L Cells

1977

The activities of the three known catabolic and the one anabolic polyadenylate enzymes have been determined in synchronized L5178y cells: endoribonuclease, exoribonuclease, 5'-nucleotidase and poly(A) polymerase (Mg2+-dependent). These four enzymes were found primarily in the nuclear fraction. The activity of poly(A) polymerase remains essentially constant during the transition from G1 to S phase. However, the poly(A) catabolic enzyme activities increase parallel with DNA synthesis; the endoribonuclease activity increases 4-fold during G1 to S phase, the exoribonuclease and the nucleotidase activities increasing 30-fold and 16-fold. During the S phase the poly(A)-degrading enzymes are far m…

Time FactorsEndoribonuclease activityEndoribonucleaseMitosisBiochemistryCell LineStructure-Activity RelationshipL CellsRibonucleasesExoribonucleaseNucleotidasePolyadenylatePolymerasechemistry.chemical_classificationbiologyDNA synthesisPolynucleotide AdenylyltransferaseNucleotidyltransferasesMolecular biologyMolecular WeightKineticsEnzymeBiochemistrychemistrybiology.proteinCell DivisionEuropean Journal of Biochemistry
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Association of AUUUA-binding Protein with A + U-rich mRNA during nucleo-cytoplasmic transport

1992

Resealed nuclear envelope (NE) vesicles from rat liver containing entrapped exogenous RNA were used to study the effect of adenosine+uridine binding factor (AUBF), present in cytosolic cell extracts, on ATP-dependent transport of A+U-rich RNA (AU+RNA) and A+U-free RNA (AU-RNA) across the NE. This factor specifically binds to A+U-rich sequences present in the 3' untranslated regions of lymphokine and cytokine mRNAs, containing overlapping AUUUA boxes (granulocyte-macrophage colony stimulating factor, interleukin-3). Addition of AUBF to the extravesicular compartment markedly increased the efflux of the in vitro transcribed, capped and polyadenylated AU+ RNAs. Export of entrapped AU- control …

Untranslated regionCytoplasmAdenosineTranscription GeneticPolyadenylationNuclear EnvelopeMolecular Sequence DataRNA-binding proteinBiologyCell LineStructural BiologyTranscription (biology)EndoribonucleasesAnimalsHumansNuclear MatrixRNA MessengerBinding siteNuclear export signalUridineMolecular BiologyCell NucleusMessenger RNABinding SitesBase SequenceGranulocyte-Macrophage Colony-Stimulating FactorInterferon-alphaRNA-Binding ProteinsRNAMolecular biologyRatsKineticsLiverRibonucleoproteinsInterleukin-3Carrier ProteinsPlasmidsPolyribonucleotidesProtein BindingJournal of Molecular Biology
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Depletion ofL-arginine induces autophagy as a cytoprotective response to endoplasmic reticulum stress in human T lymphocytes

2012

PMCID: PMC3494587

X-Box Binding Protein 1Proteasome Endopeptidase ComplexProgrammed cell deathXBP1CD3 ComplexMAP Kinase Signaling SystemRNA SplicingT-LymphocytesT cellDown-RegulationApoptosisRegulatory Factor X Transcription FactorsUbiquitin-Activating EnzymesProtein Serine-Threonine KinasesBiologyArginineLymphocyte ActivationAutophagy-Related Protein 7Jurkat cellsJurkat CellsEndoribonucleasesAutophagymedicineHumansMolecular BiologyCell ProliferationTOR Serine-Threonine KinasesAutophagyMembrane ProteinsCell BiologyBECN1Endoplasmic Reticulum StressG1 Phase Cell Cycle CheckpointsBasic Research Paper3. Good healthCell biologyDNA-Binding Proteinsmedicine.anatomical_structureCytoprotectionApoptosisUnfolded protein responseBeclin-1MitogensApoptosis Regulatory ProteinsLysosomesProto-Oncogene Proteins c-aktTranscription FactorsAutophagy
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Modulation of Nuclear Matrix-associated 2′,5′-Oligoadenylate Metabolism and Ribonuclease L Activity in H9 Cells by Human Immunodeficiency Virus

1989

Human T cells (H9), infected with the HTLV-IIIB strain of the human immunodeficiency virus (HIV-1), have been used to study the alteration of 2',5'-oligoadenylate [2'-5')A) metabolism in relation to virus production. The synthesis of (2'-5')A was determined to proceed in close association with the nuclear matrix. After HIV infection the (2'-5')A synthetase activity increased from 1.1 to 1.5 pmol of (2'-5')A synthesized/100 micrograms of nuclear matrix protein (during a 3-h in vitro incubation period) to 8.2 pmol at day 3 after infection. Then the activity dropped to the initial values. In non-infected H9 cells the (2'-5')A synthetase activity remained unchanged. Simultaneously with the decr…

biologyRNase P2'-5'-OligoadenylateEndoribonucleaseCell BiologyNuclear matrixBiochemistryVirologyVirusCell culturebiology.proteinRibonucleaseMolecular BiologyRibonuclease LJournal of Biological Chemistry
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The guanidinium group as a key part of water-soluble polymer carriers for siRNA complexation and protection against degradation.

2014

Here, the preparation of a novel block copolymer consisting of a statistical copolymer N-(2-hydroxypropyl) methacrylamide-s-N-(3-aminopropyl) methacrylamide and a short terminal 3-guanidinopropyl methacrylamide block is reported. This polymer structure forms neutral but water-soluble nanosized complexes with siRNA. The siRNA block copolymer complexes are first analyzed using agarose gel electrophoresis and their size is determined with fluorescence correlation spectroscopy. The protective properties of the polymer against RNA degradation are investigated by treating the siRNA block copolymer complexes with RNase V1. Heparin competition assays confirm the efficient release of the cargo in vi…

chemistry.chemical_classificationAcrylamidesMaterials sciencePolymers and PlasticsMicroscale thermophoresisRNase PPolymersOrganic ChemistryWaterFluorescence correlation spectroscopyPolymerchemistry.chemical_compoundchemistryAgarose gel electrophoresisPolymer chemistryEndoribonucleasesMaterials ChemistryCopolymerMethacrylamideMoleculeRNA Small InterferingGuanidineMacromolecular rapid communications
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Cooperative symmetric to asymmetric conformational transition of the apo-form of scavenger decapping enzyme revealed by simulations.

2007

Decapping is a central step in eukaryotic mRNA turnover and in gene expression regulation. The human scavenger decapping enzyme, DcpS, catalyses cap hydrolysis following mRNA degradation. DcpS is a dimeric enzyme, with two active sites. Crystal structures suggest that DcpS must undergo significant conformational changes upon ligand binding, but the mechanism of this transition is unknown. Here, we report two long timescale (20 ns) molecular dynamics simulations of the apo-form of DcpS. The dimer is observed to undergo a strikingly cooperative motion, with one active site closing while the other opens. The amplitude of the conformational change is 6–21 A and the apparent timescale is 4–13 ns…

chemistry.chemical_classificationMessenger RNAConformational changebiologyStereochemistryProtein ConformationDimerHydrolysisDCPSActive siteLigand (biochemistry)Crystallography X-RayBiochemistryCatalysisMolecular dynamicschemistry.chemical_compoundEnzymechemistryStructural BiologyEndoribonucleasesbiology.proteinHumansMolecular BiologyDimerizationProteins
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