Search results for "Ribonucleotides"

showing 10 items of 77 documents

Antisense gene therapy using anti-k-ras and antitelomerase oligonucleotides in colorectal cancer

2005

Aim: to test the efficacy of anti-k-ras and antitelomerase oligonucleotides for disabling colorectal cancer cell growth. Material and methods: an established human colorectal cancer cell line (SW 480, ATTC ® ) was used. Oligodeoxiribonucleotides (ODNs) have a phosphorotioate modification to ensure intracellular intake. We used an antitelomerase ODN (Telp5) and two anti-k-ras ODNs (AS-KRAS and ISIS). AS-KRAS is designed to join the k-ras oncogene’s exon 1. ISIS links to the terminal transcription unit 5’ of k-ras. Telp5 joins the template region of the hTR telomerase subunit. ODNs have been tested in different concentrations (1, 5, 10, 20 micromolar). Cell viability has been tested at 48 and…

TelomeraseColorectal cancerAntisense therapyK-ras oncogenemedicine.disease_causeOligodeoxyribonucleotides AntisenseCell Line TumormedicineHumansViability assayTelomeraseOligoribonucleotidesOncogeneOligonucleotideCell growthbusiness.industryGastroenterologyGenetic TherapyGeneral Medicinemedicine.diseaseColorectal cancerGenes rasImmunologyCancer researchKRASColorectal NeoplasmsbusinessSoftwareIntracellularRevista Española de Enfermedades Digestivas
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Stability of phospholipase D in primary astrocytes.

2002

Induction of expression and proteolytic breakdown of phospholipase D (PLD) isoforms in primary astrocyte cultures have been investigated. Astrocytes express both PLD1 and 2 and are dependent on PLD activity for cell proliferation [K. Kotter, J. Klein, J. Neurochem. 73 (1999) 2517]. Competitive RT-PCR analysis demonstrated a higher level of PLD1 mRNA than PLD2 mRNA (8.9 vs. 0.9amol/microg RNA, respectively). Treatment of astroglial cultures with the phorbol ester, 4beta-phorbol-12beta,13alpha-dibutyrate (0.1 microM), for 24-48h selectively induced PLD1b but not PLD1a or 2 expression as shown by PCR and Western blot; the effect was sensitive to Go 6976. In cells transiently permeabilized with…

Transcription GeneticBiophysicsCycloheximideBiologyBiochemistryGene Expression Regulation EnzymologicOligodeoxyribonucleotides Antisensechemistry.chemical_compoundWestern blotmedicinePhospholipase DAnimalsCycloheximideMolecular BiologyProtein kinase CCells CulturedPhorbol 1213-DibutyrateProtein Synthesis InhibitorsMessenger RNAmedicine.diagnostic_testPhospholipase DReverse Transcriptase Polymerase Chain ReactionPLD2BrainCell BiologyMolecular biologyCell biologyRatsIsoenzymesKineticsmedicine.anatomical_structurechemistryAnimals NewbornCytoplasmAstrocytesCell DivisionAstrocyteBiochemical and biophysical research communications
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Energy requirement and kinetics of transport of poly(A)-free histone mRNA compared to poly(A)-rich mRNA from isolated L-cell nuclei.

1989

ATP-promoted efflux of poly(A)-rich RNA from isolated nuclei of prelabeled mouse lymphoma L5178y cells has an activation energy of 51.5 kJ/mol, similar to that found for the nuclear envelope nucleoside triphosphatase (48.1 kJ/mol) assumed to be involved in mediating nucleocytoplasmic transport of at least some RNA. Here we show that efflux of two specific poly(A)-rich mRNAs (actin and beta-tubulin) from isolated L-cell nuclei is almost totally dependent on the presence of ATP, while efflux of poly(A)-free histone mRNA (H4, H2B, and H1) also occurs to a marked extent in the absence of this nucleotide. Measurements of temperature dependence of transport rate revealed an activation energy of 5…

Transcription GeneticNuclear EnvelopeRNA transportBiochemistryHistonesMiceAnimalsNucleotideRNA MessengerBinding siteLeukemia L5178Actinchemistry.chemical_classificationCell NucleusMessenger RNALeukemia ExperimentalbiologyRNANucleic Acid HybridizationRibonucleotidesBlotting NorthernMolecular biologyKineticsHistoneEnzymechemistrybiology.proteinEnergy MetabolismPoly APlasmidsEuropean journal of biochemistry
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New insights into the regulatory mechanisms of ppGpp and DksA on Escherichia coli RNA polymerase-promoter complex

2015

The stringent response modulators, guanosine tetraphosphate (ppGpp) and protein DksA, bind RNA polymerase (RNAP) and regulate gene expression to adapt bacteria to different environmental conditions. Here, we use Atomic Force Microscopy and in vitro transcription assays to study the effects of these modulators on the conformation and stability of the open promoter complex (RPo) formed at the rrnA P1, rrnB P1, its discriminator (dis) variant and lambda pR promoters. In the absence of modulators, RPo formed at these promoters show different extents of DNA wrapping which correlate with the position of UP elements. Addition of the modulators affects both DNA wrapping and RPo stability in a promo…

Transcription GeneticStringent responsemedicine.disease_causechemistry.chemical_compoundStructural BiologyRNA polymeraseGene expressionNucleotiderRNAPromoter Regions GeneticTranscription Initiation GeneticRibonucleotides/metabolismchemistry.chemical_classification0303 health sciencesDNA Bacterial/chemistry/ultrastructureEscherichia coli Proteins030302 biochemistry & molecular biologyBacterialEscherichia coli Proteins/metabolismDNA-Directed RNA PolymerasesBiological SciencesBacteriophage lambdaCell biologyEscherichia coli/enzymology/geneticsTranscriptionTranscription InitiationDNA BacterialGuanosine TetraphosphateBiologyPromoter Regions03 medical and health sciencesGeneticInformation and Computing SciencesmedicineGeneticsEscherichia coliEscherichia coli030304 developmental biologyPromoterGenes rRNADNAGene Expression Regulation BacterialRibonucleotidesequipment and suppliesMolecular biologyGuanosine TetraphosphateBacteriophage lambda/geneticschemistryGene Expression RegulationGenesbacteriaDNA-Directed RNA Polymerases/metabolismDNAEnvironmental SciencesGuanosine Tetraphosphate/metabolismDevelopmental Biology//purl.org/pe-repo/ocde/ford#1.06.07 [https]
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The yeast Aft1 transcription factor activates ribonucleotide reductase catalytic subunit RNR1 in response to iron deficiency

2020

Eukaryotic ribonucleotide reductases are iron-dependent enzymes that catalyze the rate-limiting step in the de novo synthesis of deoxyribonucleotides. Multiple mechanisms regulate the activity of ribonucleotide reductases in response to genotoxic stresses and iron deficiency. Upon iron starvation, the Saccharomyces cerevisiae Aft1 transcription factor specifically binds to iron-responsive cis elements within the promoter of a group of genes, known as the iron regulon, activating their transcription. Members of the iron regulon participate in iron acquisition, mobilization and recycling, and trigger a genome-wide metabolic remodeling of iron-dependent pathways. Here, we describe a mechanism …

Transcriptional ActivationRibonucleotideSaccharomyces cerevisiae ProteinsProtein subunitIronSaccharomyces cerevisiaeDeoxyribonucleotidesBiophysicsSaccharomyces cerevisiaeResponse ElementsBiochemistry03 medical and health sciencesStructural BiologyTranscription (biology)Gene Expression Regulation FungalRibonucleotide ReductasesGeneticsMolecular BiologyTranscription factorRibonucleotide reductase030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryIron deficiency030302 biochemistry & molecular biologyHigh Mobility Group ProteinsIron Deficienciesbiology.organism_classificationCell biologyDNA-Binding ProteinsRibonucleotide reductaseRegulonEnzymeYeast/TranscriptionProtein BindingTranscription Factors
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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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Cordycepin analogues of 2',5'-oligoadenylate inhibit human immunodeficiency virus infection via inhibition of reverse transcriptase.

1991

Analogues of 2',5'-oligoadenylates (2-5A), the cordycepin (3'-deoxyadenosine) core trimer (Co3) and its 5'-monophosphate derivative (pCo3), were shown to display pronounced anti-human immunodeficiency virus type 1 (HIV-1) activity in vitro. Treatment of HIV-1 infected H9 cells with 1 microM Co3 or pCo3 resulted in an almost 100% inhibition of virus production. The compounds were encapsulated in liposomes targeted by antibodies specific for the T-cell receptor molecule CD3. Substitution of one or two cordycepin units in Co3 or pCo3 decreased the antiviral activity of the compounds. pCo3 did not stimulate 2-5A-dependent ribonuclease L activity and displayed no effect on the amount of cellular…

Virus ReplicationBiochemistryAntiviral AgentsVirusCell Linechemistry.chemical_compoundStructure-Activity RelationshipDeoxyadenosineHumansPolymeraseNucleic Acid Synthesis InhibitorsOligoribonucleotidesbiologyCordycepinDeoxyadenosines2'-5'-OligoadenylateAdenine NucleotidesRNAMolecular biologyReverse transcriptaseBiochemistrychemistryRNA RibosomalLiposomesbiology.proteinHIV-1RNA Transfer LysReverse Transcriptase InhibitorsRibonuclease LBiochemistry
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RNA dependent DNA polymerase in cells of xeroderma pigmentosum

1971

Abstract Cells from X.P. ∗ skin contain an RNA dependent DNA polymerase, while in cells from normal skin this enzyme is lacking. This finding stimulates the thought that carcinogenesis in X.P. cells is due to an infection with an oncogenic RNA virus.

Xeroderma pigmentosumHepatitis B virus DNA polymeraseDNA polymeraseDNA polymerase IIDeoxyribonucleotidesPolynucleotidesBiophysicsRNA-dependent RNA polymeraseTritiummedicine.disease_causeRauscher VirusBiochemistryMicemedicineAnimalsChemical PrecipitationHumansMolecular BiologySkinchemistry.chemical_classificationXeroderma Pigmentosumintegumentary systembiologyRNA virusDNATemplates GeneticCell BiologyRibonucleotidesmedicine.diseasebiology.organism_classificationVirologyMolecular biologyStimulation ChemicalEnzymechemistryAmmonium SulfateDNA Nucleotidyltransferasesbiology.proteinRNAFemaleGuanosine TriphosphateCarcinogenesisBiochemical and Biophysical Research Communications
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Application of a weakly basic dimethylamino-modified silica ion exchanger to the separation of oligonucleotides

1979

Abstract LiChrosorb RP-8, RP-18 and Diol as well as a newly synthesized basic dimethylamino-modified silica ion-exchanger (DMA-silica) were applied for the separation of adenylic acid, cytidylic acid and uridylic acid oligoribonucleotides. On LiChrosorb RP-8 and RP-18, respectively, in aqueous buffered eluents (K 2 HPO 4 - H 3 PO 4 ), the retention of oligonucleotides was increased with decreasing number of nucleotide units in the solute, i.e., with increasing hydrophobic character. The elution behaviour of ologonucleotides on LiChrosorb Diol followed the same order but took place according to a size-exclusion mechanism. The retention of oligonucleotides on DMA-silica is assumed to be based…

chemistry.chemical_classificationChromatographyAqueous solutionIon exchangeElutionOrganic ChemistryDiolIonic bondingSalt (chemistry)General MedicineBiochemistryAnalytical Chemistrychemistry.chemical_compoundchemistryOligoribonucleotidesNucleotideJournal of Chromatography A
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Kinetic properties of a nucleoside phosphotransferase of chick embryo

1981

1. A nonspecific nucleoside phosphotransferase (nucleotide : 3'-deoxynucleotide 5'-phosphotransferase, EC 2.7.1.77), purified from chick embryos, catalyzes the transfer of phosphate ester from a nucleotide donor to a nucleoside acceptor. 2. The enzyme exhibits sigmoidal kinetics with respect to nucleoside monophosphate donors, but with respect to nucleoside di- or triphosphate donors and nucleoside acceptors hyperbolic kinetics were obtained. 3. The nucleoside phosphotransferase of chick embryo is unstable to heat and is protected from inactivation by a large number of nucleosides. 4. Nucleoside di- and triphosphates lower both the concentration of nucleoside monophosphates required for hal…

chemistry.chemical_classificationHot TemperatureDeoxyribonucleotidesPhosphotransferasesKineticsNucleosidesGeneral MedicineRibonucleotidesNucleotidyltransferaseUridine DiphosphateNucleoside-diphosphate kinasePhosphotransferaseKineticsEnzymeDrug StabilitychemistryBiochemistrySettore BIO/10 - BiochimicaNucleoside phosphotransferaseAnimalsNucleotidechick embryoNucleoside
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