Search results for "Nucleoside-Triphosphatase"

showing 5 items of 5 documents

Binding and/or hydrolysis of purine‐based nucleotides is not required for IM30 ring formation

2021

IM30, the inner membrane-associated protein of 30 kDa, is conserved in cyanobacteria and chloroplasts. Although its exact physiological function is still mysterious, IM30 is clearly essential for thylakoid membrane biogenesis and/or dynamics. Recently, a cryptic IM30 GTPase activity has been reported, albeit thus far no physiological function has been attributed to this. Yet, it is still possible that GTP binding/hydrolysis affects formation of the prototypical large homo-oligomeric IM30 ring and rod structures. Here, we show that the Synechocystis sp. PCC 6803 IM30 protein in fact is an NTPase that hydrolyzes GTP and ATP, but not CTP or UTP, with about identical rates. While IM30 forms lar…

GTP'Genetic VectorsBiophysicsGene ExpressionGTPaseRing (chemistry)ThylakoidsBiochemistrySubstrate Specificity03 medical and health sciencesAdenosine TriphosphateBacterial ProteinsStructural BiologyEscherichia coliGeneticsNucleotideddc:610Cloning MolecularMolecular BiologyEnzyme Assays030304 developmental biologychemistry.chemical_classification0303 health sciencesbiologyChemistryHydrolysis030302 biochemistry & molecular biologySynechocystisSynechocystisMembrane ProteinsCell BiologyNucleoside-Triphosphatasebiology.organism_classificationRecombinant ProteinsKineticsMicroscopy ElectronThylakoidMembrane biogenesisBiophysicsGuanosine TriphosphateBiogenesisProtein BindingFEBS Letters
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Modulation of the nuclear-envelope nucleoside triphosphatase by poly(A)-rich mRNA and by microtubule protein.

1982

Nuclear envelopes contain a nucleoside triphosphatase which is thought to be involved in the supply of energy for nucleo-cytoplasmic RNA transport. This enzyme is stimulated most efficiently by poly(A) and to a lesser extent by poly(G) and poly(dT). Half-maximal stimulation of the enzyme from rat liver nuclei, which was associated with the poly(A)-specific endoribonuclease IV and was free from poly(A) polymerase and endoribonuclease V activity, was determined to occur at a concentration of 1.1 × 106 poly(A) molecules/nuclear ghost. Double-reciprocal plot analyses revealed a 2.8-fold stimulation of the enzyme by poly(A). Poly(A) in the hybrid form had no influence on the activity of the nucl…

MaleNuclear EnvelopeEndoribonucleaseRNA transportIn Vitro TechniquesBiochemistryPolydeoxyribonucleotidesTubulinAnimalsNucleotideRNA MessengerPolymerasechemistry.chemical_classificationMessenger RNAbiologyRNABiological TransportRats Inbred StrainsNucleoside-TriphosphataseEnzyme assayActinsPhosphoric Monoester HydrolasesRatsEnzyme ActivationTubulinchemistryBiochemistrybiology.proteinPoly APolyribonucleotidesEuropean journal of biochemistry
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Differential effect of insulin and epidermal growth factor on the mRNA translocation system and transport of specific poly(A+) mRNA and poly(A-) mRNA…

1990

The efficiency of efflux of rapidly labeled poly(A)-containing mRNA from isolated rat liver nuclei was found to be modulated by insulin and epidermal growth factor (EGF) in a biphasic but opposite way. At physiological concentrations (10 pM insulin and 1 pM EGF), maximal stimulation of the transport rate by insulin (to 137%) and maximal inhibition by EGF (to 69%) were obtained; at higher concentrations (greater than 100 pM and greater than 10 pM, respectively), the amount of poly(A)-containing mRNA released into the postnuclear supernatant was nearly identical with the level found in untreated nuclei (= 100%). Using mRNA entrapped into closed nuclear envelope (NE) vesicles as a model system…

MaleNuclear Envelopemedicine.medical_treatmentPhosphoprotein phosphatase activityBiologyBiochemistryDephosphorylationAdenosine TriphosphateEpidermal growth factormedicineCyclic AMPMRNA transportAnimalsInsulinRNA MessengerBinding sitePhosphorylationCyclic GMPCell NucleusMessenger RNAEpidermal Growth FactorInsulinBiological TransportRats Inbred StrainsBlotting NorthernNucleoside-TriphosphataseMolecular biologyPhosphoric Monoester HydrolasesRatsKineticsPhosphorylationPoly ABiochemistry
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Proteins from rat liver cytosol which stimulate mRNA transport. Purification and interactions with the nuclear envelope mRNA translocation system.

1986

Two polysome-associated proteins with particular affinities for poly(A) have been purified from rat liver. These proteins stimulate the efflux of mRNA from isolated nuclei in conditions under which such efflux closely stimulates mRNA transport in vivo, and they are therefore considered as mRNA-transport-stimulatory proteins. Their interaction with the mRNA-translocation system in isolated nuclear envelopes has been studied. The results are generally consistent with the most recently proposed kinetic model of mRNA translocation. One protein, P58, has not been described previously. It inhibits the protein kinase that down-regulates the NTPase, it enhances the NTPase activity in both the prese…

MaleNucleocytoplasmic Transport ProteinsNuclear EnvelopeRNA-binding proteinBiologyBiochemistryCytosolPhosphoprotein PhosphatasesMRNA transportAnimalsRNA MessengerProtein kinase AMessenger RNANucleocytoplasmic Transport ProteinsRNARNA-Binding ProteinsBiological TransportRats Inbred StrainsNucleoside-TriphosphatasePhosphoric Monoester HydrolasesCell biologyRatsCytosolBiochemistryLiverPolyribosomesPhosphorylationCarrier ProteinsPoly AProtein KinasesEuropean journal of biochemistry
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Evidence for a direct interaction of Rev protein with nuclear envelop mRNA-translocation system.

1991

The interaction of the Rev protein from human immunodeficiency virus type 1 (HIV-1) with the nucleocytoplasmic mRNA-transport system was investigated. In gel-shift assay, the recombinant Rev protein used in this study selectively bound to the Rev-responsive element (RRE) region of HIV-1 env-specific RNA. Nitrocellulose-filter-binding studies and Northern/Western-blotting experiments revealed an association constant of approximately 1 x 10(10) M-1. The Rev protein also strongly bound to isolated nuclear envelopes from H9 cells, containing the poly(A)-binding site (= mRNA carrier) and the nucleoside triphosphatase (= NTPase), which are thought to be involved in nuclear export of poly(A)-rich …

Pore complexPolyadenylationNuclear EnvelopevirusesBlotting WesternBiologyBiochemistryCell LineAdenosine TriphosphateAnimalsRNA MessengerNuclear porePhosphorylationNuclear export signalMessenger RNAVesicleRNABiological Transportrev Gene Products Human Immunodeficiency VirusBlotting NorthernNucleoside-TriphosphataseMolecular biologyPhosphoric Monoester HydrolasesRecombinant ProteinsCell biologyRatsBlotGene Products revHIV-1RNA ViralPoly AEuropean journal of biochemistry
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