2023
Mistranslation of the genetic code by a new family of bacterial transfer RNAs
Schuntermann D, Fischer J, Bile J, Gaier S, Shelley B, Awawdeh A, Jahn M, Hoffman K, Westhof E, Söll D, Clarke C, Vargas-Rodriguez O. Mistranslation of the genetic code by a new family of bacterial transfer RNAs. Journal Of Biological Chemistry 2023, 299: 104852. PMID: 37224963, PMCID: PMC10404621, DOI: 10.1016/j.jbc.2023.104852.Peer-Reviewed Original ResearchConceptsTransfer RNAsAmino acidsBacterial transfer RNAsUnfavorable environmental conditionsProlyl-tRNA synthetaseWrong amino acidPoor substrate specificitySubstrate discriminationGrowth defectTransfer RNAGenetic codePosttranslational modificationsProtein reporterTranslation factorsEnvironmental stressFunctional proteinsSubstrate specificityThreonine codonGenetic informationDistinct isoformsPro mutationAntibiotic carbenicillinEscherichia coliNovel familyEnvironmental conditions
2012
Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment
Ling J, Peterson KM, Simonović I, Cho C, Söll D, Simonović M. Yeast mitochondrial threonyl-tRNA synthetase recognizes tRNA isoacceptors by distinct mechanisms and promotes CUN codon reassignment. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 3281-3286. PMID: 22343532, PMCID: PMC3295322, DOI: 10.1073/pnas.1200109109.Peer-Reviewed Original ResearchMeSH KeywordsAeropyrumAmino Acid SequenceAnticodonCatalytic DomainCodonCrystallography, X-RayEscherichia coliEvolution, MolecularLeucineMitochondriaModels, MolecularMolecular Sequence DataProtein ConformationProtein Structure, TertiaryRNA EditingRNA, Transfer, Amino AcylSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence AlignmentSpecies SpecificityStaphylococcus aureusSubstrate SpecificityThreonineThreonine-tRNA LigaseConceptsThreonyl-tRNA synthetaseAnticodon loopAnticodon sequenceEscherichia coli ThrRSSet of tRNAsDistinct recognition mechanismsAnticodon-binding domainAminoacyl-tRNA synthetasesCUN codonsDetailed structural comparisonCodon reassignmentYeast mitochondriaGenetic codeTRNA isoacceptorsSaccharomyces cerevisiaeIsoacceptor tRNAsEditing domainTRNAMST1Anticodon tripletStructural comparisonNatural tRNAAmino acidsDistinct mechanismsRecognition mechanism
2011
An unusual tRNAThr derived from tRNAHis reassigns in yeast mitochondria the CUN codons to threonine
Su D, Lieberman A, Lang BF, Simonović M, Söll D, Ling J. An unusual tRNAThr derived from tRNAHis reassigns in yeast mitochondria the CUN codons to threonine. Nucleic Acids Research 2011, 39: 4866-4874. PMID: 21321019, PMCID: PMC3113583, DOI: 10.1093/nar/gkr073.Peer-Reviewed Original ResearchConceptsCUN codonsYeast mitochondriaGenetic codeAlloacceptor tRNA gene recruitmentComprehensive phylogenetic analysisStandard genetic codeThreonyl-tRNA synthetaseHistidyl-tRNA synthetaseGene recruitmentEvolutionary originPhylogenetic analysisRecoding eventBiochemical experimentsFirst nucleotideAnticodon loopMST1CodonFirst clear exampleYeastMitochondriaThreonineSynthetaseCandida albicansGenomeClear example
2006
Structure of the unusual seryl‐tRNA synthetase reveals a distinct zinc‐dependent mode of substrate recognition
Bilokapic S, Maier T, Ahel D, Gruic‐Sovulj I, Söll D, Weygand‐Durasevic I, Ban N. Structure of the unusual seryl‐tRNA synthetase reveals a distinct zinc‐dependent mode of substrate recognition. The EMBO Journal 2006, 25: 2498-2509. PMID: 16675947, PMCID: PMC1478180, DOI: 10.1038/sj.emboj.7601129.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acid SequenceAnimalsArchaeal ProteinsBinding SitesCrystallography, X-RayDimerizationEnzyme ActivationHumansMethanosarcina barkeriModels, MolecularMolecular Sequence DataMolecular StructureProtein Structure, QuaternarySequence AlignmentSequence Homology, Amino AcidSerineSerine-tRNA LigaseSubstrate SpecificityThreonineConceptsSeryl-tRNA synthetaseTRNA-binding domainMinimal sequence similarityResolution crystal structureAmino acid substratesActive site zinc ionSequence similaritySubstrate recognitionSerRSsSerine substrateMotif 1Methanogenic archaeaMutational analysisProtein ligandsEnzymatic activityArchaeaAminoacyl-tRNA synthetase systemsDistinct mechanismsAbsolute requirementRecognition mechanismSynthetase systemSynthetaseIon ligandsZinc ionsEucaryotes
2002
tRNA‐dependent amino acid discrimination by yeast seryl‐tRNA synthetase
Gruic‐Sovulj I, Landeka I, Söll D, Weygand‐Durasevic I. tRNA‐dependent amino acid discrimination by yeast seryl‐tRNA synthetase. The FEBS Journal 2002, 269: 5271-5279. PMID: 12392560, DOI: 10.1046/j.1432-1033.2002.03241.x.Peer-Reviewed Original ResearchConceptsSeryl-tRNA synthetaseYeast seryl-tRNA synthetaseCognate tRNA moleculesAmino acid discriminationAminoacyl-tRNA synthetasesAmino acid substratesSimilar amino acidsAmino acid serineGenetic codeEnzyme active siteTRNA moleculesActive siteYeast SerRSConformational changesAcid substratesAmino acidsSerineSynthetaseStoichiometric analysisDifferent affinitiesEnzymeAccurate translationTRNASerSynthetasesSaccharomyces
1974
N‐(purin‐6‐ylcarbamoyl)threonine: Biosynthesis in vitro in transfer RNA by an enzyme purified from Escherichia coli
Körner A, Söll D. N‐(purin‐6‐ylcarbamoyl)threonine: Biosynthesis in vitro in transfer RNA by an enzyme purified from Escherichia coli. FEBS Letters 1974, 39: 301-306. PMID: 4604806, DOI: 10.1016/0014-5793(74)80135-3.Peer-Reviewed Original ResearchMeSH KeywordsAlkaline PhosphataseAmino Acyl-tRNA SynthetasesCarbamatesCarbon RadioisotopesChromatography, DEAE-CelluloseChromatography, Ion ExchangeChromatography, PaperChromatography, Thin LayerElectrophoresis, PaperEscherichia coliIsotope LabelingMutationNitrosoguanidinesPhosphorus RadioisotopesPurine NucleosidesRibonucleasesRNA, BacterialRNA, TransferSpectrophotometry, UltravioletThreonineTime FactorsTritium
1972
Is There a Discriminator Site in Transfer RNA?
Crothers D, Seno T, Söll D. Is There a Discriminator Site in Transfer RNA? Proceedings Of The National Academy Of Sciences Of The United States Of America 1972, 69: 3063-3067. PMID: 4562753, PMCID: PMC389707, DOI: 10.1073/pnas.69.10.3063.Peer-Reviewed Original Research
1968
Biosynthesis of the Peptidoglycan of Bacterial Cell Walls VI. Incorporation Of l-Threonine Into Interpeptide Bridges in Micrococcus Roseus
Roberts W, Strominger J, Söll D. Biosynthesis of the Peptidoglycan of Bacterial Cell Walls VI. Incorporation Of l-Threonine Into Interpeptide Bridges in Micrococcus Roseus. Journal Of Biological Chemistry 1968, 243: 749-756. PMID: 5638591, DOI: 10.1016/s0021-9258(19)81729-5.Peer-Reviewed Original Research