1990
Purification and functional characterization of the Glu-tRNA(Gln) amidotransferase from Chlamydomonas reinhardtii.
Jahn D, Kim Y, Ishino Y, Chen M, Söll D. Purification and functional characterization of the Glu-tRNA(Gln) amidotransferase from Chlamydomonas reinhardtii. Journal Of Biological Chemistry 1990, 265: 8059-8064. PMID: 1970821, DOI: 10.1016/s0021-9258(19)39038-6.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmmoniaAsparagineAzo CompoundsBinding SitesChlamydomonasElectrophoresis, Polyacrylamide GelEnzyme ActivationGlutamatesGlutamic AcidGlutamineMagnesiumMolecular WeightNitrogenous Group TransferasesNorleucinePhosphorylationProtein DenaturationRNA, Transfer, Amino AcylSpectrophotometrySubstrate SpecificityTransferasesConceptsChlamydomonas reinhardtiiGlutamyl-tRNA synthetaseGlycerol gradient sedimentationSodium dodecyl sulfate-polyacrylamide gelsDodecyl sulfate-polyacrylamide gelsAmide donorSulfate-polyacrylamide gelsGlutamine-dependent reactionGlutamine amidotransferasesPresence of ATPGreen algaeSpecific amidotransferaseFunctional characterizationGlutaminyl-tRNAAmidotransferaseLow glutaminase activityApparent MrGradient sedimentationAlpha 2 structureReinhardtiiEnzymeATPGlutaminase activityStable complexesAmmonia-dependent reaction
1972
Properties of a dimer of tRNA I Tyr 1 (Escherichia coli).
Yang S, Söll D, Crothers D. Properties of a dimer of tRNA I Tyr 1 (Escherichia coli). Biochemistry 1972, 11: 2311-20. PMID: 4555033, DOI: 10.1021/bi00762a016.Peer-Reviewed Original ResearchAmino Acyl-tRNA SynthetasesCarbon IsotopesChemical PhenomenaChemistryChemistry, PhysicalEscherichia coliHot TemperatureKineticsMacromolecular SubstancesMagnesiumMathematicsModels, ChemicalModels, StructuralNucleic Acid ConformationNucleic Acid DenaturationNucleic Acid HybridizationRNA, BacterialRNA, TransferSodiumSpectrophotometryTemperatureThermodynamicsTyrosineUltracentrifugationUltraviolet Rays
1971
Temperature dependence of the aminoacylation of tRNA by bacillus stearothermophilus aminoacyl‐tRNA synthetases
Johnson L, Söll D. Temperature dependence of the aminoacylation of tRNA by bacillus stearothermophilus aminoacyl‐tRNA synthetases. Biopolymers 1971, 10: 2209-2221. PMID: 4940767, DOI: 10.1002/bip.360101114.Peer-Reviewed Original ResearchConceptsSpecific transfer RNAsTRNA-IleTransfer RNAThermal denaturation profilesB. stearothermophilusAminoacyl-tRNA synthetasesDenaturation profilesAminoacylation of tRNAAmino acid acceptor activityTRNA-ValAcceptor activityTRNATertiary structureMycoplasma spBacillus stearothermophilusEscherichia coliAminoacylation reactionStearothermophilusAminoacylationRNASpeciesIleSynthetasesNucleaseSynthetase preparations