2010
Structure of an archaeal non-discriminating glutamyl-tRNA synthetase: a missing link in the evolution of Gln-tRNAGln formation
Nureki O, O’Donoghue P, Watanabe N, Ohmori A, Oshikane H, Araiso Y, Sheppard K, Söll D, Ishitani R. Structure of an archaeal non-discriminating glutamyl-tRNA synthetase: a missing link in the evolution of Gln-tRNAGln formation. Nucleic Acids Research 2010, 38: 7286-7297. PMID: 20601684, PMCID: PMC2978374, DOI: 10.1093/nar/gkq605.Peer-Reviewed Original ResearchConceptsNon-discriminating glutamyl-tRNA synthetaseGlutamyl-tRNA synthetaseND-GluRSEscherichia coli GlnRSFormation of GlnCognate tRNA moleculesGlutaminyl-tRNA synthetaseAnticodon-binding domainEvolutionary predecessorPhylogenetic analysisGenetic codeMolecular basisTRNA moleculesRecognition pocketGlnRGenetic encodingAmino acidsSpecific ligationStructural determinantsKey eventsSynthetaseGluPromiscuous recognitionGluRGln
2006
A Molecular Tunnel Required for Cooperation of an Asparaginase and a Glu‐tRNAGln Kinase in Gln‐tRNA Formation
Sheppard K, Feng L, Oshikane H, Nakamura Y, Fukai S, Nureki O, Söll D. A Molecular Tunnel Required for Cooperation of an Asparaginase and a Glu‐tRNAGln Kinase in Gln‐tRNA Formation. The FASEB Journal 2006, 20: a503-a503. DOI: 10.1096/fasebj.20.4.a503-a.Peer-Reviewed Original ResearchGlu-tRNAGlnMolecular tunnelMost prokaryotesCo-crystal structurePresence of ATPGln-tRNAGlnSequence similarityEvolutionary linkHeterodimeric enzymeStructural insightsGatDEGatDEnzyme showEnzymatic analysisKinaseAmide donorCrystal structureActive siteATPGlnGluProkaryotesArchaeaTransamidationTight coupling
2000
The heterotrimeric Thermus thermophilus Asp‐tRNAAsn amidotransferase can also generate Gln‐tRNAGln
Becker H, Min B, Jacobi C, Raczniak G, Pelaschier J, Roy H, Klein S, Kern D, Söll D. The heterotrimeric Thermus thermophilus Asp‐tRNAAsn amidotransferase can also generate Gln‐tRNAGln. FEBS Letters 2000, 476: 140-144. PMID: 10913601, DOI: 10.1016/s0014-5793(00)01697-5.Peer-Reviewed Original Research
1996
Transfer RNA‐dependent cognate amino acid recognition by an aminoacyl‐tRNA synthetase.
Hong K, Ibba M, Weygand‐Durasevic I, Rogers M, Thomann H, Söll D. Transfer RNA‐dependent cognate amino acid recognition by an aminoacyl‐tRNA synthetase. The EMBO Journal 1996, 15: 1983-1991. PMID: 8617245, PMCID: PMC450117, DOI: 10.1002/j.1460-2075.1996.tb00549.x.Peer-Reviewed Original ResearchConceptsAmino acid recognitionEscherichia coli glutaminyl-tRNA synthetaseAccuracy of aminoacylationProtein-RNA interactionsRole of tRNAGlutaminyl-tRNA synthetaseAmino acid affinityCharacterization of mutantsAminoacyl-tRNA synthetaseAmino acid activationSpecific interactionsSubstrate recognitionEnzyme active siteGlnRActive siteAcceptor stemTRNAAminoacylationAcid affinityPosition 235TerminusSynthetaseObserved roleGlnTRNAGln
1988
Accuracy of in Vivo Aminoacylation Requires Proper Balance of tRNA and Aminoacyl-tRNA Synthetase
Swanson R, Hoben P, Sumner-Smith M, Uemura H, Watson L, Söll D. Accuracy of in Vivo Aminoacylation Requires Proper Balance of tRNA and Aminoacyl-tRNA Synthetase. Science 1988, 242: 1548-1551. PMID: 3144042, DOI: 10.1126/science.3144042.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthetaseAminoacyl-tRNA synthetasesProtein biosynthesisAccuracy of aminoacylationCognate aminoacyl-tRNA synthetaseAmber suppressorVivo aminoacylationGln-tRNA synthetaseCognate tRNATRNAExquisite specificityAminoacylationSynthetaseAccurate aminoacylationSynthetasesBiosynthesisIntracellular concentrationRelative levelsProper balanceComplexed formsSuppressorEscherichiaGlnProtein biosynthesis in organelles requires misaminoacylation of tRNA
Schön A, Kannangara C, Cough S, SÖll D. Protein biosynthesis in organelles requires misaminoacylation of tRNA. Nature 1988, 331: 187-190. PMID: 3340166, DOI: 10.1038/331187a0.Peer-Reviewed Original ResearchConceptsProtein biosynthesisOrigin of organellesCrude chloroplast extractAnimal mitochondriaRNA involvementSpecific amidotransferaseTRNA speciesConversion of glutamateBarley chloroplastsChloroplast extractsProtein synthesisTRNAOrganellesSpeciesChloroplastsAminoacylation studiesBiosynthesisAmide donorGlutamineGlnCyanobacteriaAmidotransferaseMisaminoacylationMitochondriaOrganisms
1985
Two control systems modulate the level of glutaminyl-tRNA synthetase in Escherichia coli
Cheung A, Watson L, Söll D. Two control systems modulate the level of glutaminyl-tRNA synthetase in Escherichia coli. Journal Of Bacteriology 1985, 161: 212-218. PMID: 2578447, PMCID: PMC214858, DOI: 10.1128/jb.161.1.212-218.1985.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseEscherichia coli glutaminyl-tRNA synthetaseBeta-galactosidase structural genePost-transcriptional regulationStructural geneTranscriptional controlRegulatory mutationsTranslational levelGln-10Metabolic regulationEscherichia coliSynthetaseVivo expressionTranscriptionGrowth conditionsRegulationMRNA levelsRegulatory studiesSynthetase levelsMutationsGlnGrowth rateGenesPromoterColi
1984
In vivo and in vitro transcription of the Escherichia coli glutaminyl-tRNA synthetase gene.
Cheung A, Söll D. In vivo and in vitro transcription of the Escherichia coli glutaminyl-tRNA synthetase gene. Journal Of Biological Chemistry 1984, 259: 9953-9958. PMID: 6086662, DOI: 10.1016/s0021-9258(17)42791-8.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseGlutaminyl-tRNA synthetase geneTranslation initiation codon AUGInitiation codon AUGPresence of tRNATermination codon UAAGlnS geneTerminator structureTranscription initiationSynthetase geneTranscription initiatesCodons UAARegulatory signalsCodon AUGTermination sitesTranscription productsSequence analysisStructure upstreamStructural regionsTranscriptionGenesTranscriptsSynthetaseMRNAGln
1979
Regulation of the biosynthesis of aminoacyl-transfer ribonucleic acid synthetases and of transfer ribonucleic acid in Escherichia coli. VI. Mutants with increased levels of glutaminyl-transfer ribonucleic acid synthetase and of glutamine transfer ribonucleic acid
Cheung A, Morgan S, Low K, Söll D. Regulation of the biosynthesis of aminoacyl-transfer ribonucleic acid synthetases and of transfer ribonucleic acid in Escherichia coli. VI. Mutants with increased levels of glutaminyl-transfer ribonucleic acid synthetase and of glutamine transfer ribonucleic acid. Journal Of Bacteriology 1979, 139: 176-184. PMID: 378954, PMCID: PMC216843, DOI: 10.1128/jb.139.1.176-184.1979.Peer-Reviewed Original ResearchConceptsTransfer ribonucleic acidAminoacyl-transfer ribonucleic acid synthetasesE. coli mapGlutaminyl-tRNA synthetaseRibonucleic acidTRNA-GlnStructural geneGenetic lociEscherichia coli strainsSpontaneous revertantsEscherichia coliParental strainThermolabile enzymeInteresting strainsColi strainsSynthetaseLociRevertantsEnzymeGlnMin 24GlnRStrainsTRNAMutants
1974
Isolation and Partial Characterization of a Temperature-Sensitive Escherichia coli Mutant with Altered Glutaminyl-Transfer Ribonucleic Acid Synthetase
Körner A, Magee B, Liska B, Low K, Adelberg E, Söll D. Isolation and Partial Characterization of a Temperature-Sensitive Escherichia coli Mutant with Altered Glutaminyl-Transfer Ribonucleic Acid Synthetase. Journal Of Bacteriology 1974, 120: 154-158. PMID: 4153616, PMCID: PMC245744, DOI: 10.1128/jb.120.1.154-158.1974.Peer-Reviewed Original Research