Search results for "Uridine"

showing 10 items of 142 documents

The purification and properties of nucleoside phosphotransferase from mucosa of chicken intestine

1984

Abstract (1) Nucleoside phosphotransferase (nucleotide:3′-deoxynucleoside 5′-phosphotransferase, EC 2.7.1.77) has been purified from chicken intestine mucosa to apparent homogeneity. The enzyme is represented by a multisubunit protein at different degrees of association. It can dissociate into a compoenent with a marked fall in catalytic activity. (2) The associated forms are similar to the enzyme previously purified from chick embryo as regards: substrate specificity both with respect to nucleoside monophosphate donors and to deoxyribonucleoside acceptors; sigmoidicity in the rate curve with a variable phosphate donor; instability to heat, dilution and lowering of pH; the activating and pr…

StereochemistryCations DivalentProtein subunitBiophysicsBiologyBiochemistrychemistry.chemical_compoundStructural BiologySettore BIO/10 - BiochimicaNucleoside phosphotransferaseCentrifugation Density GradientAnimalsUreaNucleotideEnzyme kineticsIntestinal MucosaMolecular Biologychemistry.chemical_classificationNucleotidesPhosphotransferasesPhosphatenucleoside phosphotransferaseDeoxyuridineDeoxyribonucleosideMolecular WeightKineticsEnzymechemistryBiochemistryAlcoholsChromatography GelElectrophoresis Polyacrylamide GelChickens
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Eukaryotic tRNAs(Pro): primary structure of the anticodon loop; presence of 5-carbamoylmethyluridine or inosine as the first nucleoside of the antico…

1990

The modified nucleoside U*, located in the first position of the anticodon of yeast, chicken liver and bovine liver tRNA(Pro) (anticodon U*GG), has been determined by means of TLC, HPLC, ultraviolet spectrum and gas chromatography-mass spectrometry. The structure was established as 5-carbamoylmethyluridine (ncm5U). In addition, we report on the primary structures of the above-mentioned tRNAs as well as those which have the IGG anticodon. In yeast, the two tRNA(Pro) (anticodons U*GG and IGG) differ by eight nucleotides, whereas in chicken and in bovine liver, both anticodons are carried by the same 'body tRNA' with one posttranscriptional exception at position 32, where pseudouridine is asso…

StereochemistryMolecular Sequence DataBiophysicsBiologyBiochemistryPseudouridinechemistry.chemical_compoundRNA Transfer ProRNA TransferStructural BiologyYeastsGeneticsmedicineAnticodonAnimalsNucleotideInosineUridinechemistry.chemical_classificationChromatographyBase SequenceMolecular StructureProtein primary structureFungal geneticsRNARNA FungalRNA Transfer Amino Acid-SpecificInosinechemistryBiochemistryTransfer RNANucleic Acid ConformationCattleSpectrophotometry UltravioletNucleosideChickensmedicine.drugBiochimica et biophysica acta
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Structural Basis and Enzymatic Mechanism of the Biosynthesis of C9- from C10-Monoterpenoid Indole Alkaloids

2009

Cutting carbons: The three-dimensional structure of polyneuridine aldehyde esterase (PNAE) gives insight into the enzymatic mechanism of the biosynthesis of C(9)- from C(10)-monoterpenoid indole alkaloids (see scheme). PNAE is a very substrate-specific serine esterase. It harbors the catalytic triad S87-D216-H244, and is a new member of the alpha/beta-fold hydrolase superfamily. Its novel function leads to the diversification of alkaloid structures.

Stereochemistrychemistry [Secologanin Tryptamine Alkaloids]polyneuridine aldehyde esterasePolyneuridine-aldehyde esteraseCatalysisSubstrate SpecificityEnzyme catalysischemistry.chemical_compoundProtein structureBiosynthesisHydrolaseCatalytic triadmetabolism [Mutant Proteins]Indole testchemistry.chemical_classificationGeneral ChemistrySecologanin Tryptamine AlkaloidsProtein Structure Tertiarymetabolism [Carboxylic Ester Hydrolases]metabolism [Secologanin Tryptamine Alkaloids]EnzymeAmino Acid SubstitutionchemistryBiochemistryddc:540BiocatalysisMutant ProteinsCarboxylic Ester HydrolasesAngewandte Chemie International Edition
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Studies on sea urchin oocytes. II. Synthesis of RNA during oogenesis.

1972

Abstract Isolated oocytes of the sea urchin Paracentrotus lividus actively incorporate 3H-uridine into RNA. Labeled RNA was analysed by sucrose gradient and acrylamide gel electrophoresis following cell fractionation. Much of the radioactivity is incorporated at the nucleolar level in the form of rRNA precursors. The kinetics of maturation of these latter suggests that this occurs at a slower rate than during embryogenesis. Other non-nucleolar RNA classes are also actively labelled and retained in the nucleus for many hours. These results are confirmed by an autoradiographic investigation.

SucroseTime FactorsBiologyCell FractionationTritiumOogenesisParacentrotus lividusbiology.animalBotanyCentrifugation Density GradientAnimalsPolyacrylamide gel electrophoresisSea urchinUridineOvumCell NucleusHistocytochemistryEmbryogenesisRNACell BiologyRibosomal RNAbiology.organism_classificationElectrophoresis DiscMolecular WeightBiochemistryRNA RibosomalSea UrchinsAutoradiographyRNAFemaleCell fractionationCell NucleolusExperimental cell research
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Kti12, a PSTK-like tRNA dependent ATPase essential for tRNA modification by Elongator

2019

Abstract Posttranscriptional RNA modifications occur in all domains of life. Modifications of anticodon bases are of particular importance for ribosomal decoding and proteome homeostasis. The Elongator complex modifies uridines in the wobble position and is highly conserved in eukaryotes. Despite recent insights into Elongator's architecture, the structure and function of its regulatory factor Kti12 have remained elusive. Here, we present the crystal structure of Kti12′s nucleotide hydrolase domain trapped in a transition state of ATP hydrolysis. The structure reveals striking similarities to an O-phosphoseryl-tRNA kinase involved in the selenocysteine pathway. Both proteins employ similar …

TRNA modificationSaccharomyces cerevisiae ProteinsProtein ConformationWobble base pairSaccharomyces cerevisiaeBiologyChaetomiumCrystallography X-Ray03 medical and health scienceschemistry.chemical_compound0302 clinical medicineRNA TransferATP hydrolysisGeneticsRNA and RNA-protein complexesAnticodonRNA Processing Post-TranscriptionalUridine030304 developmental biologyAdaptor Proteins Signal TransducingAdenosine Triphosphatases0303 health sciencesSelenocysteineRNATRNA bindingCell biologychemistryTransfer RNASelenocysteine incorporationCarrier ProteinsRibosomes030217 neurology & neurosurgery
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CRMP-4 expression in the adult cerebral cortex and other telencephalic areas of the lizard Podarcis hispanica.

2002

The control of neuritogenesis is crucial for the development, maturation and regeneration of the nervous system. The collapsin response-mediated protein 4 (CRMP-4) is a member of a family of proteins that are involved in neuronal differentiation and axonal outgrowth. In rodents, this protein is expressed in recently generated neurons such as some granule neurons of the dentate gyrus, as well as in certain differentiated neurons undergoing neurite outgrowth or synaptogenesis during adulthood. Since CRMP-4 protein appears to be highly conserved throughout the evolutionary scale, we have used immunocytochemistry to study its distribution in the lizard cerebral cortex. We have found pronounced …

TelencephalonNeuriteMedial cortexGrowth ConesSynaptogenesisNerve Tissue ProteinsPodarcis hispanicaEvolution MolecularDevelopmental NeurosciencemedicineAnimalsCerebral CortexbiologyDentate gyrusStem CellsNeurogenesisCell DifferentiationLizardsbiology.organism_classificationImmunohistochemistrymedicine.anatomical_structurenervous systemBromodeoxyuridineCerebral cortexDentate GyrusNeuroscienceNucleusCell DivisionDevelopmental BiologyBrain research. Developmental brain research
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Ras, Rap, and Rac Small GTP-binding Proteins Are Targets for Clostridium sordellii Lethal Toxin Glucosylation

1996

Lethal toxin (LT) from Clostridium sordellii is one of the high molecular mass clostridial cytotoxins. On cultured cells, it causes a rounding of cell bodies and a disruption of actin stress fibers. We demonstrate that LT is a glucosyltransferase that uses UDP-Glc as a cofactor to covalently modify 21-kDa proteins both in vitro and in vivo. LT glucosylates Ras, Rap, and Rac. In Ras, threonine at position 35 was identified as the target amino acid glucosylated by LT. Other related members of the Ras GTPase superfamily, including RhoA, Cdc42, and Rab6, were not modified by LT. Incubation of serum-starved Swiss 3T3 cells with LT prevents the epidermal growth factor-induced phosphorylation of m…

ThreonineUridine Diphosphate GlucoseRHOABacterial ToxinsMolecular Sequence DataClostridium sordelliimacromolecular substancesCDC42GTPaseBiologyCell morphologyBiochemistryGTP PhosphohydrolasesProto-Oncogene Proteins p21(ras)MiceGTP-binding protein regulatorsGTP-Binding ProteinsAnimalsHumansAmino Acid SequenceMolecular BiologyClostridiumEpidermal Growth FactorKinase3T3 CellsCell Biologybiology.organism_classificationMolecular biologyActinsrac GTP-Binding ProteinsActin CytoskeletonKineticsGlucoserap GTP-Binding ProteinsGlucosyltransferasesCalcium-Calmodulin-Dependent Protein Kinasesbiology.proteinPhosphorylationGuanosine TriphosphateHeLa CellsJournal of Biological Chemistry
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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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Cellular UDP-Glucose Deficiency Caused by a Single Point Mutation in the UDP-Glucose Pyrophosphorylase Gene

1997

We previously isolated a mutant cell that is the only mammalian cell reported to have a persistently low level of UDP-glucose. In this work we obtained a spontaneous revertant whose UDP-glucose level lies between those found in the wild type and the mutant cell. The activity of UDP-glucose pyrophosphorylase (UDPG:PP), the enzyme that catalyzes the formation of UDP-glucose, was in the mutant 4% and in the revertant 56% of the activity found in the wild type cell. Sequence analysis of UDPG: PP cDNAs from the mutant cell showed one missense mutation, which changes amino acid residue 115 from glycine to aspartic acid. The substituted glycine is located within the largest stretch of strictly con…

Uridine Diphosphate GlucoseDNA ComplementaryMagnetic Resonance SpectroscopyUTP-Glucose-1-Phosphate UridylyltransferaseMolecular Sequence DataMutantDeoxyglucoseBiologymedicine.disease_causeBiochemistryProtein Structure SecondaryCell LineCricetulusCricetinaeAspartic acidmedicineAnimalsPoint MutationMissense mutationAmino Acid SequenceMolecular Biologychemistry.chemical_classificationMutationSequence Homology Amino AcidPoint mutationWild typeCell BiologyMolecular biologyEnzymeBiochemistrychemistryGlycineJournal of Biological Chemistry
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High yielding one-pot enzyme-catalyzed synthesis of UDP-glucose in gram scales

2001

Abstract Uridine diphosphoglucose is an important cofactor of glucosylating enzymes. A simple and high yielding one-pot enzymatic synthesis of UDPG on a gram scale from glucose via hexokinase, phosphoglucomutase and UDPG pyrophosphorylase (UGPase) is described. Repetitive addition of substrate was used to avoid inhibition of UGPase. The approach allows recovery of active enzymes and their re-use. The synthesis of UDP-[4-13C]-glucose on a 0.5 g scale resulted in a final yield of 70% and a purity of >95% after chromatographic purification.

Uridine Diphosphate GlucoseMagnetic Resonance SpectroscopyUTP-Glucose-1-Phosphate UridylyltransferaseBiochemistryHigh yieldingCatalysisCofactorAnalytical Chemistrychemistry.chemical_compoundHexokinaseCarbon RadioisotopesGramchemistry.chemical_classificationHexokinaseChromatographyMolecular StructurebiologyOrganic ChemistrySubstrate (chemistry)General MedicineGlucoseEnzymePhosphoglucomutasechemistryBiochemistryYield (chemistry)biology.proteinPhosphoglucomutaseCarbohydrate Research
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