Search results for "Poly U"

showing 4 items of 4 documents

Association of a polyuridylate-specific endoribonuclease with small nuclear ribonucleo-proteins which had been isolated by affinity chromatography us…

1983

Immunoglobulins, containing antibodies against U1-snRNP, have been prepared from a patient with systemic lupus erythematosus. After coupling these antibodies to a Sepharose matrix, U-snRNPs have been isolated and purified from rat liver nuclei by use of immunoaffinity chromatography. The resulting RNPs had the typical protein pattern of U-sn RNPs and a sedimentation coefficient of 12 S. The U-snRNP preparation was associated with an endoribonuclease which required Mg2+ for optimal activity. The enzyme, with an pH optimum of 6.2, degraded only poly(U). Other single-stranded polyribo- and polydeoxyribonucleotides, tRNA, as well as double-stranded RNA and DNA were not digested. The products of…

MalePoly UEndoribonucleaseAntibody AffinityBiologyenvironment and public healthBiochemistryChromatography AffinitySubstrate SpecificitySepharosechemistry.chemical_compoundAffinity chromatographyEndoribonucleasesAnimalsHumansLupus Erythematosus Systemicchemistry.chemical_classificationImmunochemistryRNARats Inbred StrainsRibonucleoproteins Small NuclearMolecular biologyRatsEnzymechemistryLiverRibonucleoproteinsAntibodies AntinuclearImmunoglobulin GRNA splicingTransfer RNADNAEuropean journal of biochemistry
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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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Genetic Analysis of Sequences in the 3′ Nontranslated Region of Hepatitis C Virus That Are Important for RNA Replication

2002

ABSTRACT The genome of the hepatitis C virus (HCV) is a plus-strand RNA molecule that carries a single long open reading frame. It is flanked at either end by highly conserved nontranslated regions (NTRs) that mediate crucial steps in the viral life cycle. The 3′ NTR of HCV has a tripartite structure composed of an about 40-nucleotide variable region, a poly(U/UC) tract that has a heterogeneous length, and a highly conserved 98-nucleotide 3′-terminal sequence designated the X tail or 3′X. Conflicting data as to the role the sequences in the 3′ NTR play in RNA replication have been reported. By using the HCV replicon system, which is based on the self-replication of subgenomic HCV RNAs in hu…

Poly URNA StabilityHepatitis C virusImmunologyMolecular Sequence DataRNA-dependent RNA polymeraseReplicationHepacivirusBiologymedicine.disease_causeMicrobiologychemistry.chemical_compoundVirologymedicineTumor Cells CulturedHumansReplicon3' Untranslated RegionsSubgenomic mRNAGeneticsBase SequenceThree prime untranslated regionRNAVirologychemistryMutagenesisInsect ScienceNucleic Acid ConformationRNA ViralCytosine
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Poly(U) RNA-templated synthesis of AppA.

2015

Simple nucleotide templating activities are of interest as potential primordial reactions. Here we describe the acceleration of 5′-5′ AppA synthesis by 3′-5′ poly(U) under normal solution conditions. This reaction is apparently templated via complementary U:A base-pairing, despite the involvement of two different RNA backbones, because poly(U), unlike other polymers, significantly stimulates AppA synthesis. These interactions occur in moderate (K+) and (Mg2+) and are temperature sensitive, being more efficient at 10°C than at 4°C, but absent at 20°C. The reaction is only slightly pH sensitive, despite potentially relevant substrate pKa’s. Kinetic data explicitly support production of AppA b…

chemistry.chemical_classificationPoly UbiologyMolecular modelStereochemistryRNASubstrate (chemistry)Chemical reactionCofactorArticlechemistryBiochemistrybiology.proteinMoleculeRNANucleotideMolecular BiologyDinucleoside PhosphatesDinucleoside PhosphatesRNA (New York, N.Y.)
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