Search results for "GTP'"

showing 10 items of 21 documents

Selective Stimulation of Hepatitis C Virus and Pestivirus NS5B RNA Polymerase Activity by GTP

1999

NS5B of the hepatitis C virus is an RNA template-dependent RNA polymerase and therefore the key player of the viral replicase complex. Using a highly purified enzyme expressed with recombinant baculoviruses in insect cells, we demonstrate a stimulation of RNA synthesis up to 2 orders of magnitude by high concentrations of GTP but not with ATP, CTP, UTP, GDP, or GMP. Enhancement of RNA synthesis was found with various heteropolymeric RNA templates, with poly(C)-oligo(G)12 but not with poly(A)-oligo(U)12. Several amino acid substitutions in polymerase motifs B, C, and D previously shown to be crucial for RdRp activity were tested for GTP stimulation of RNA synthesis. Most of these mutations, …

GTP'biologyvirusesRNA-dependent RNA polymeraseRNADNA-Directed RNA PolymerasesHepacivirusCell BiologyViral Nonstructural ProteinsRNA-Dependent RNA PolymeraseBiochemistryMolecular biologyPost-transcriptional modificationEnzyme Activationchemistry.chemical_compoundchemistryRNA polymerasePestivirusbiology.proteinRNA polymerase IRNA ViralGuanosine TriphosphateMolecular BiologyPolymeraseSmall nuclear RNAJournal of Biological Chemistry
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PURINE AND PYRIMIDINE NUCLEOTIDES IN THE BRAIN OF NORMAL AND CONVULSANT RATS

1969

— Purine and pyrimidine nucleotides were measured in the brain of normal and electroshocked rats after chromatographic separation on ion-exchange resin of mono-, di- and tri-phosphorylated derivatives. CMP, IMP and NAD did not show any significant quantitative change. Adenine nucleotides showed an abrupt change followed by a rapid return to the control value. GTP was the only purine nucleotide exhibiting a relatively slow return to its starting concentration. The greatest percentage increase after electroshock was observed in UMP, which returned to its control value only after 5 min; UDPCoenzymes (i.e. UDPA plus UDPG) showed a relatively small drop during the development of the seizure and …

MalePurineGTP'Uracil NucleotidesCytosine NucleotidesTritiumBiochemistryCellular and Molecular Neurosciencechemistry.chemical_compoundAdenosine TriphosphateSeizuresAdenine nucleotideAnimalsNucleotidechemistry.chemical_classificationChromatographyElectroshockAdenine NucleotidesNucleotidesChemistryBrainNADGuanine NucleotidesUridineRatsPyrimidinesBiochemistryPurinesConvulsantIon Exchange ResinsNAD+ kinasePyrimidine NucleotidesJournal of Neurochemistry
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Structural insights into the GTPase domain of Escherichia coli MnmE protein

2007

The Escherichia coli MnmE protein is a 50-kDa multidomain GTPase involved in tRNA modification. Its homologues in eukaryotes are crucial for mitochondrial respiration and, thus, it is thought that the human protein might be involved in mitochondrial diseases. Unlike Ras, MnmE shows a high intrinsic GTPase activity and requires effective GTP hydrolysis, and not simply GTP binding, to be functionally active. The isolated MnmE G-domain (165 residues) conserves the GTPase activity of the entire protein, suggesting that it contains the catalytic residues for GTP hydrolysis. To explore the GTP hydrolysis mechanism of MnmE, we analyzed the effect of low pH on binding and hydrolysis of GTP, as well…

Models MolecularTRNA modificationMagnetic Resonance SpectroscopyGTP'aluminium fluoridehomology modelingMolecular Sequence DataGTPaseGuanosine triphosphateGuanosine DiphosphateBiochemistryeraGTP Phosphohydrolaseschemistry.chemical_compoundStructural BiologyEscherichia coliAmino Acid SequenceHomology modelingBinding siteGTPaseMolecular BiologyBinding SitesSequence Homology Amino AcidChemistryEscherichia coli ProteinsTrmENMRRecombinant ProteinsKineticsBiochemistryMnmEGuanosine diphosphateRap2AGTP PhosphohydrolasesGuanosine TriphosphateSequence AlignmentRasProteins: Structure, Function, and Bioinformatics
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Restoration of Clostridium difficile toxin-B-inhibited phospholipase D by phosphatidylinositol 4,5-bisphosphate.

1996

Receptor signalling to phospholipase D (PLD) in human embryonic kidney (HEK) cells stably expressing the m3 muscarinic acetylcholine receptor apparently involves Rho proteins. Since phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2] has been recognized as an essential cofactor for PLD activity and since activated Rho proteins have been reported to stimulate the synthesis of PtdIns(4,5)P2, we studied whether in HEK cells PLD activity is regulated by PtdIns(4,5)P2 and, in particular, whether PtdIns(4,5)P2 can restore PLD activity inhibited by Clostridium difficile toxin B, which inactivates Rho proteins. Addition of MgATP to permeabilized HEK cells increased basal PLD activity and potentia…

Phosphatidylinositol 45-DiphosphateGTP'Bacterial ToxinsClostridium difficile toxin BBiologyBiochemistryCell Linechemistry.chemical_compoundBacterial ProteinsGTP-Binding ProteinsPhosphatidylcholineRhoB GTP-Binding ProteinPhospholipase DHumansPhosphatidylinositolEnzyme InhibitorsrhoB GTP-Binding ProteinPhospholipase DClostridioides difficileHEK 293 cellsCell MembraneMembrane ProteinsReceptors MuscarinicCell biologyEnzyme Activationenzymes and coenzymes (carbohydrates)chemistryPhosphatidylinositol 45-bisphosphateGuanosine 5'-O-(3-Thiotriphosphate)lipids (amino acids peptides and proteins)European journal of biochemistry
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Differential changes in purine nucleotides after Doxorubicin treatment of human cancer cells in vitro

2002

The present investigation was performed to elucidate the role of purine nucleotides as potential indicators of chemosensitivity of malignant tumors. Drug-sensitive (s) and -resistant (r) tumor cell lines grown as monolayers (s: T47D, MCF-7 wild-type; r: NCI/ADR-RES, MCF-7/MDR) or as multicellular spheroids (T47D; NCI/ADR-RES) were exposed to 0.1, 1.0, and 10.0 microM Doxorubicin for up to 24 h. Purine nucleotides were assayed using HPLC and with some selected spheroids using imaging bioluminescence. The data show that in the time frame of the experiments reproducible and statistically significant changes in the nucleotides only occur at the highest drug concentration investigated. Under the…

PurineCancer ResearchOligomycinGTP'Antineoplastic AgentsIn Vitro TechniquesBiologychemistry.chemical_compoundAdenosine TriphosphateIn vivoSpheroids CellularTumor Cells CulturedmedicineHumansNucleotideDoxorubicinATP Binding Cassette Transporter Subfamily B Member 1Chromatography High Pressure Liquidchemistry.chemical_classificationBiological activityMolecular biologyDrug Resistance MultipleIn vitroOncologyBiochemistrychemistryDoxorubicinDrug Resistance NeoplasmLuminescent MeasurementsGuanosine Triphosphatemedicine.drugInternational Journal of Oncology
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Nucleotide pool changes in coelomic cells (eleocytes) of the polychaete Nereis virens during sexual maturation

1998

Eleocytes (a type of coelomic cell) of the polychaete Nereis virens can store large amounts of adenine nucleotides at certain times. Since eleocytes have specific functions related to gametogenesis, we tested whether the presence of these large nucleotide stores in eleocytes is specific to gender or related to specific events during gametogenesis. Nucleotide pools in eleocytes isolated at different stages of sexual maturation from N. virens were analysed using high-performance liquid chromatography. Eleocytes from immature and male animals had extremely high concentrations of both AMP and ADP (each > 10 µmol/ml of packed cell volume). In eleocytes from male animals, the high nucleotide stor…

Purinechemistry.chemical_classificationGTP'Biologychemistry.chemical_compoundmedicine.anatomical_structurechemistryBiochemistryAdenine nucleotideNucleic acid biosynthesismedicineNucleic acidNucleotideGerm cellGametogenesis
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Antagonistic feedback loops involving Rau and Sprouty in the Drosophila eye control neuronal and glial differentiation.

2013

During development, differentiation is often initiated by the activation of different receptor tyrosine kinases (RTKs), which results in the tightly regulated activation of cytoplasmic signaling cascades. In the differentiation of neurons and glia in the developing Drosophila eye, we found that the proper intensity of RTK signaling downstream of fibroblast growth factor receptor (FGFR) or epidermal growth factor receptor required two mutually antagonistic feedback loops. We identified a positive feedback loop mediated by the Ras association (RA) domain-containing protein Rau that sustained Ras activity and counteracted the negative feedback loop mediated by Sprouty. Rau has two RA domains t…

Receptors SteroidGTP'Blotting WesternIn situ hybridizationEyeBiochemistryReceptor tyrosine kinaseMicroscopy Electron TransmissionAnimalsDrosophila ProteinsEpidermal growth factor receptorReceptorMolecular BiologyTranscription factorIn Situ HybridizationFeedback PhysiologicalbiologyIntracellular Signaling Peptides and ProteinsMembrane ProteinsReceptor Protein-Tyrosine KinasesCell DifferentiationCell BiologyAnatomyPhenotypeImmunohistochemistryCell biologyProtein Structure TertiaryDNA-Binding ProteinsEnzyme ActivationCOUP Transcription FactorsGene Expression RegulationFibroblast growth factor receptorbiology.proteinDrosophilaNeurogliaProtein BindingSignal TransductionScience signaling
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The GTP- and Phospholipid-Binding Protein TTD14 Regulates Trafficking of the TRPL Ion Channel in Drosophila Photoreceptor Cells

2015

Recycling of signaling proteins is a common phenomenon in diverse signaling pathways. In photoreceptors of Drosophila, light absorption by rhodopsin triggers a phospholipase Cβ-mediated opening of the ion channels transient receptor potential (TRP) and TRP-like (TRPL) and generates the visual response. The signaling proteins are located in a plasma membrane compartment called rhabdomere. The major rhodopsin (Rh1) and TRP are predominantly localized in the rhabdomere in light and darkness. In contrast, TRPL translocates between the rhabdomeral plasma membrane in the dark and a storage compartment in the cell body in the light, from where it can be recycled to the plasma membrane upon subsequ…

RhodopsinCancer Researchlcsh:QH426-470LightGTP'BiologyEye03 medical and health sciencesTransient receptor potential channelTransient Receptor Potential Channels0302 clinical medicineGTP-binding protein regulatorsGTP-Binding ProteinsGeneticsAnimalsDrosophila ProteinsMolecular BiologyGenetics (clinical)Ecology Evolution Behavior and SystematicsIon channel030304 developmental biology0303 health sciencesCell MembraneMembrane ProteinsDarknessRhabdomereTransport proteinCell biologylcsh:GeneticsProtein TransportDrosophila melanogasterMembrane proteinRhodopsinMutationbiology.proteinPhotoreceptor Cells Invertebrate030217 neurology & neurosurgerySignal TransductionResearch ArticlePLOS Genetics
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Role of glycine-82 as a pivot point during the transition from the inactive to the active form of the yeast Ras2 protein

1991

AbstractRas proteins bind either GDP or GTP with high affinity. However, only the GTP-bound form of the yeast Ras2 protein is able to stimulate adenylyl cyclase. To identify amino acid residues that play a role in the conversion from the GDP-bound to the GTP-bound state of Ras proteins, we have searched for single amino acid substitutions that selectively affected the binding of one of the two nucleotides. We have found that the replacement of glycine-82 of the Ras2 protein by serine resulted in an increased rate of dissociation of Gpp(NH)p, a nonhydrolysable analog of GTP, while the GDP dissociation rate was not significantly modified. Glycine-82 resides in a region that is highly conserve…

Saccharomyces cerevisiae ProteinsGTP'Guanosine diphosphateProtein ConformationRestriction MappingGlycineBiophysicsSaccharomyces cerevisiaeBiochemistryFungal ProteinsGTP-binding protein regulatorsProtein structureGTP-Binding ProteinsStructural BiologyEscherichia coliGeneticsRHO protein GDP dissociation inhibitorAmino Acid SequenceRas2Binding siteMolecular BiologyPeptide sequencechemistry.chemical_classificationGuanylyl ImidodiphosphateBinding SitesPoint mutationChemistryCell BiologyGuanosine triphosphateRecombinant ProteinsAmino acidModels StructuralBiochemistryMutagenesis Site-Directedras ProteinsS. cerevisaePlasmidsRasFEBS Letters
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Phosphorylation of an Overexpressed Yeast Ras2 Protein During the G1 Phase of the Cell Cycle

1994

RAS proteins regulate growth and differentiation in evolutionarily distant systems such as vertebrates and yeast (for reviews, see Tamanoi, 1988; Gibbs and Marshall, 1989; Broach and Deschenes, 1990). At the moleular level, a key function of the yeast RAS1 and RAS2 proteins (collectively referred to as RAS) is to positively regulate the production of cyclic AMP at the onset of the G1 phase of the cell cycle (Toda et al., 1985; De Vendittis et al., 1986). At this stage, RAS proteins are transiently activated by the noncovalent binding of a GTP molecule. Reversal of the effect occurs by the hydrolytic splitting of the ’γ-phosphate of GTP, that leaves a functionally inactive RASGDP complex, th…

SerineCyclin-dependent kinase 1GTP'ChemistryImmunoprecipitationPhosphorylationRas2Cell cycleYeastCell biology
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