2010
Mutations Disrupting Selenocysteine Formation Cause Progressive Cerebello-Cerebral Atrophy
Agamy O, Zeev B, Lev D, Marcus B, Fine D, Su D, Narkis G, Ofir R, Hoffmann C, Leshinsky-Silver E, Flusser H, Sivan S, Söll D, Lerman-Sagie T, Birk OS. Mutations Disrupting Selenocysteine Formation Cause Progressive Cerebello-Cerebral Atrophy. American Journal Of Human Genetics 2010, 87: 538-544. PMID: 20920667, PMCID: PMC2948803, DOI: 10.1016/j.ajhg.2010.09.007.Peer-Reviewed Original Research
2008
Quality control despite mistranslation caused by an ambiguous genetic code
Ruan B, Palioura S, Sabina J, Marvin-Guy L, Kochhar S, LaRossa RA, Söll D. Quality control despite mistranslation caused by an ambiguous genetic code. Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 16502-16507. PMID: 18946032, PMCID: PMC2575449, DOI: 10.1073/pnas.0809179105.Peer-Reviewed Original ResearchConceptsGenetic codeAa-tRNAWild-type proteinAminoacyl-tRNA synthetasesInactive mutant proteinsHeat shock responseE. coliMutant proteinsReporter proteinMissense suppressionFunctional proteinsCognate tRNASelective pressureAminoacyl-tRNAActive enzymeShock responseProtein synthesisNative conformationEnergetic costAmino acidsMissense mutationsProteinBiochemical evidenceCorrect pairingProtein quality
1997
Glutamyl-tRNA sythetase.
Freist W, Gauss D, Söll D, Lapointe J. Glutamyl-tRNA sythetase. Biological Chemistry 1997, 378: 1313-29. PMID: 9426192.Peer-Reviewed Original ResearchConceptsGlutamyl-tRNA synthetaseGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesNegative eubacteriaBacterial glutamyl-tRNA synthetasesATP/PPiHigh molecular mass complexesClass I aminoacyl-tRNA synthetasesCytoplasm of eukaryotesE. coli GlnRSGlutamyl-tRNA synthetasesMolecular mass complexesN-terminal halfC-terminal halfAmino acid residuesDihydrouridine (DHU) armPhylogenetic studiesSpecific amidotransferaseGlutamyl-prolylMass complexesTRNA synthetasesCognate tRNAAcid residuesAcceptor stemSynthetasesGlutaminyl-tRNA synthetase.
Freist W, Gauss D, Ibba M, Söll D. Glutaminyl-tRNA synthetase. Biological Chemistry 1997, 378: 1103-17. PMID: 9372179.Peer-Reviewed Original ResearchConceptsE. coli GlnRSGlutaminyl-tRNA synthetaseGlutamyl-tRNA synthetaseMammalian enzymeCommon ancestorPositive eubacteriaCognate tRNAMultienzyme complexTRNA moleculesGlnRArtificial mutantsAcceptor stemAnticodon loopMolecular massAmino acidsCatalytic siteEnzymeSynthetaseEubacteriaArchaebacteriaTRNAMutantsOrganellesAncestorComplexes
1996
Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme.
Ibba M, Hong K, Sherman J, Sever S, Söll D. Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 6953-6958. PMID: 8692925, PMCID: PMC38915, DOI: 10.1073/pnas.93.14.6953.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesAnimalsBase SequenceBinding SitesCalorimetryCloning, MolecularConsensus SequenceEscherichia coliHumansKineticsModels, StructuralMolecular Sequence DataNucleic Acid ConformationProtein FoldingRecombinant ProteinsRNA, Transfer, GlnSequence Homology, Nucleic AcidConceptsGlutaminyl-tRNA synthetaseAmino acid affinityAmino acid recognitionEscherichia coli glutaminyl-tRNA synthetaseBase pairsIdentity nucleotidesProtein-RNA interactionsDiscriminator baseE. coli tryptophanyl-tRNA synthetaseAminoacyl-tRNA synthetasesSequence-specific interactionsAcid affinityRecognition sitesAbility of tRNATryptophanyl-tRNA synthetaseTRNA specificityNoncognate substratesTranslational fidelityTRNA recognitionBiochemical functionsRNA recognitionCognate tRNATRNAMajor binding siteNoncognate tRNAs
1995
Substrate selection by aminoacyl-tRNA synthetases.
Ibba M, Thomann H, Hong K, Sherman J, Weygand-Durasevic I, Sever S, Stange-Thomann N, Praetorius M, Söll D. Substrate selection by aminoacyl-tRNA synthetases. Nucleic Acids Symposium Series 1995, 40-2. PMID: 8643392.Peer-Reviewed Original Research
1994
Recognition in the Glutamine tRNA System: from Structure to Function
Sherman J, Rogers M, Söll D. Recognition in the Glutamine tRNA System: from Structure to Function. 1994, 395-409. DOI: 10.1128/9781555818333.ch19.Peer-Reviewed Original ResearchEscherichia coli glutaminyl-tRNA synthetaseFirst high-resolution crystal structureAccurate protein synthesisProtein-RNA interactionsImportant specificity determinantsProtein-RNA complexesClose evolutionary relationshipE. coli GlnRSGlutaminyl-tRNA synthetaseHigh-resolution crystal structuresGlutamyl-tRNA synthetaseAminoacyl-tRNA synthetasesRecognition of tRNAEvolutionary relationshipsTRNA identity elementsTight recognitionSpecificity determinantsTRNA substratesGlnRBiochemical approachesCognate tRNATRNA systemTRNABiophysical techniquesEnzyme mechanismIdentity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases.
Frugier M, Söll D, Giegé R, Florentz C. Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases. Biochemistry 1994, 33: 9912-21. PMID: 8060999, DOI: 10.1021/bi00199a013.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthetasesIdentity nucleotidesHigh-resolution X-ray structuresAminoacyl-tRNA synthetase complexGlutaminyl-tRNA synthetaseAspartyl-tRNA synthetasesAspartyl-tRNA synthetaseGlutamine identityCognate tRNATRNA structureTRNA moleculesTRNAAminoacylation specificitySynthetase complexSpecific aminoacylationConformational changesSynthetasesEscherichia coliYeastSynthetaseNucleotidesE. coliX-ray structureComplex formationColi
1992
Aminoacyl-tRNA synthetase-induced cleavage of tRNA
Beresten S, Jahn M, Söll D. Aminoacyl-tRNA synthetase-induced cleavage of tRNA. Nucleic Acids Research 1992, 20: 1523-1530. PMID: 1579445, PMCID: PMC312233, DOI: 10.1093/nar/20.7.1523.Peer-Reviewed Original Research
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 formsSuppressorEscherichiaGln
1972
Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli II. INTERACTION WITH INTACT GLUTAMYL TRANSFER RIBONUCLEIC ACID
Lapointe J, Söll D. Glutamyl Transfer Ribonucleic Acid Synthetase of Escherichia coli II. INTERACTION WITH INTACT GLUTAMYL TRANSFER RIBONUCLEIC ACID. Journal Of Biological Chemistry 1972, 247: 4975-4981. PMID: 4341532, DOI: 10.1016/s0021-9258(19)44926-0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acyl-tRNA SynthetasesCarbon IsotopesCatalysisCentrifugation, Density GradientDiphosphatesDrug StabilityEscherichia coliGlutamatesHot TemperatureHydrogen-Ion ConcentrationKineticsLeucineMagnesiumPhosphorus IsotopesProtein BindingRNA, TransferSpectrometry, FluorescenceValineConceptsGlutamyl-transfer ribonucleic acid synthetaseEscherichia coli IITransfer ribonucleic acidTRNA-GluTRNA-ValTRNA-LeuCognate tRNABiological specificityRibonucleic acidPure enzymeEnzymeSimilar Km valuesComplex formationGradient centrifugationSynthetaseKm valuesFluorescence-quenching studiesTRNAIsoacceptorsComplexesFluorescence quenching studiesHeat inactivationInactivationLeuGlu
1970
The Interaction of Seryl and of Leucyl Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids
Knowles J, Katze J, Konigsberg W, Söll D. The Interaction of Seryl and of Leucyl Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids. Journal Of Biological Chemistry 1970, 245: 1407-1415. PMID: 4910800, DOI: 10.1016/s0021-9258(18)63251-x.Peer-Reviewed Original ResearchConceptsSeryl-tRNA synthetaseTransfer ribonucleic acidComplex formationTransfer RNA speciesLeucyl-tRNA synthetaseRibonucleic acidRNA speciesCognate tRNAEscherichia coliSynthetaseDensity gradient centrifugationTRNAStable complexesHigh saltGradient centrifugationSpeciesGel filtrationComplexesSerylColiATPEnzymeAcidSerFormation