2022
Uncovering translation roadblocks during the development of a synthetic tRNA
Prabhakar A, Krahn N, Zhang J, Vargas-Rodriguez O, Krupkin M, Fu Z, Acosta-Reyes FJ, Ge X, Choi J, Crnković A, Ehrenberg M, Puglisi EV, Söll D, Puglisi J. Uncovering translation roadblocks during the development of a synthetic tRNA. Nucleic Acids Research 2022, 50: 10201-10211. PMID: 35882385, PMCID: PMC9561287, DOI: 10.1093/nar/gkac576.Peer-Reviewed Original ResearchConceptsOrthogonal translation systemGenetic code expansionCode expansionTertiary interactionsNon-canonical amino acidsAminoacyl-tRNA substratesDomains of lifeAminoacyl-tRNA synthetaseTranslation systemSingle nucleotide mutationsSingle-molecule fluorescenceDistinct tRNAsNon-canonical structuresSelenocysteine insertionRibosomal translationTRNARibosomesSynthetic tRNANucleotide mutationsAmino acidsSame organismP siteOrganismsTranslocationTranslation
2010
1SE1020 Genetic code extension and establishment by aminoacyl-tRNA synthetase and tRNA modification enzymes(1SE Recent Advances in Structural Analyses of Funcitonal Mechanisms Based on Dynamics of Biological Reactions,The 48th Annual Meeting of the Biophysical Society of Japan)
Nakanishi K, Bonnefond L, Nozawa K, Soll D, Suzuki T, Ishitani R, Nureki O. 1SE1020 Genetic code extension and establishment by aminoacyl-tRNA synthetase and tRNA modification enzymes(1SE Recent Advances in Structural Analyses of Funcitonal Mechanisms Based on Dynamics of Biological Reactions,The 48th Annual Meeting of the Biophysical Society of Japan). Seibutsu Butsuri 2010, 50: s3. DOI: 10.2142/biophys.50.s3_5.Peer-Reviewed Original ResearchGenetic code extensionAminoacyl-tRNA synthetase
2007
Features of Aminoacyl‐tRNA Synthesis Unique to Archaea
Polycarpo C, Sheppard K, Randau L, Ambrogelly A, Cardoso A, Fukai S, Herring S, Hohn M, Nakamura Y, Oshikane H, Palioura S, Salazar J, Yuan J, Nureki O, Söll D. Features of Aminoacyl‐tRNA Synthesis Unique to Archaea. 2007, 198-208. DOI: 10.1128/9781555815516.ch9.Peer-Reviewed Original ResearchAminoacyl-tRNA synthetasesAmino acidsCognate tRNA speciesCorrect amino acidDomains of lifeAminoacyl-tRNA synthetaseIntron-exon junctionsCorresponding tRNAsNanoarchaeum equitansMethylated thiolsM. jannaschiiMature tRNATRNA speciesGenomic studiesAncient familyBulge motifCysteine synthesisMethanogenic archaeaArchaeaBiosynthetic routeAa-tRNATRNATwo-step pathwayCys-tRNACysSynthetases
2006
Mischarging of M. barkeri tRNAPyl with alanine and serine in vitro
Li D, Polycarpo C, Ambrogelly A, Söll D. Mischarging of M. barkeri tRNAPyl with alanine and serine in vitro. The FASEB Journal 2006, 20: a503-a503. DOI: 10.1096/fasebj.20.4.a503-c.Peer-Reviewed Original ResearchNon-canonical amino acidsSecondary structureCognate tRNA speciesPyrrolysyl-tRNA synthetaseAminoacyl-tRNA synthetaseSimilar secondary structureBovine mitochondriaTRNA speciesAlanine tRNAAnticodon stemAcceptor stemAmino acidsM. barkeriMethanosarcina barkeriSerRSsPyrrolysineMultiple mutationsVariable loopSynthetaseSerineShorter variable loopsSynthetase systemBarkeriAlanineStem
2001
Cysteinyl-tRNA synthetase is not essential for viability of the archaeon Methanococcus maripaludis
Stathopoulos C, Kim W, Li T, Anderson I, Deutsch B, Palioura S, Whitman W, Söll D. Cysteinyl-tRNA synthetase is not essential for viability of the archaeon Methanococcus maripaludis. Proceedings Of The National Academy Of Sciences Of The United States Of America 2001, 98: 14292-14297. PMID: 11717392, PMCID: PMC64675, DOI: 10.1073/pnas.201540498.Peer-Reviewed Original ResearchConceptsCysteinyl-tRNA synthetaseMethanococcus maripaludisArchaeon Methanococcus maripaludisLateral gene transferNormal growth conditionsAminoacyl-tRNA synthetasesAminoacyl-tRNA synthetaseArchaea Methanocaldococcus jannaschiiProlyl-tRNA synthetaseCysS genesCys-tRNAMethanocaldococcus jannaschiiM. maripaludisSynthetase geneIntriguing enzymeMethanothermobacter thermautotrophicusCysteinyl-tRNAKnockout strainProlyl-tRNAGene transferSynthetaseBiochemical analysisVivo translationGrowth conditionsCysRS
2000
A dual-specificity aminoacyl-tRNA synthetase in the deep-rooted eukaryote Giardia lamblia
Bunjun S, Stathopoulos C, Graham D, Min B, Kitabatake M, Wang A, Wang C, Vivarès C, Weiss L, Söll D. A dual-specificity aminoacyl-tRNA synthetase in the deep-rooted eukaryote Giardia lamblia. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 12997-13002. PMID: 11078517, PMCID: PMC27167, DOI: 10.1073/pnas.230444397.Peer-Reviewed Original ResearchConceptsCys-tRNAAminoacyl-tRNA synthetaseProlyl-tRNA synthetasePrimitive eukaryote Giardia lambliaPro geneEukaryote Giardia lambliaNumber of archaeaAlanyl-tRNA synthetasesCysteinyl-tRNA synthetaseE. coli tRNACysS genesM. jannaschiiMethanococcus jannaschiiMost organismsGenomic sequencesSaccharomyces cerevisiaeCysteinyl-tRNAGene productsPro-tRNATRNA synthetaseDual specificityMethanobacterium thermoautotrophicumProtein synthesisEscherichia coliAmino acidsAMINOACYL-tRNA SYNTHESIS
Ibba M, Söll D. AMINOACYL-tRNA SYNTHESIS. Annual Review Of Biochemistry 2000, 69: 617-650. PMID: 10966471, DOI: 10.1146/annurev.biochem.69.1.617.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthesisAmino acidsAminoacyl-tRNA synthetaseEvolutionary facetsWhole-genome sequencingCorresponding tRNAsGenetic codeGenome sequencingAminoacyl-tRNACorresponding anticodonTRNACurrent knowledgeStructural dataRecent studiesAnticodonDetailed pictureAcidSequencingSynthetaseEditingProofreadingSynthesisTranslationDirect attachment
1997
A Euryarchaeal Lysyl-tRNA Synthetase: Resemblance to Class I Synthetases
Ibba M, Morgan S, Curnow A, Pridmore D, Vothknecht U, Gardner W, Lin W, Woese C, Söll D. A Euryarchaeal Lysyl-tRNA Synthetase: Resemblance to Class I Synthetases. Science 1997, 278: 1119-1122. PMID: 9353192, DOI: 10.1126/science.278.5340.1119.Peer-Reviewed Original ResearchConceptsClass I aminoacyl-tRNA synthetaseCrenarchaeote Sulfolobus solfataricusDinucleotide-binding domainAminoacyl-tRNA synthetasesAmino acid motifsAmino acid sequenceAminoacyl-tRNA synthetaseLysyl-tRNA synthetaseClass II synthetasesEuryarchaeal genomesUnassigned functionMethanococcus jannaschiiMethanococcus maripaludisLysRS proteinsReading frameSulfolobus solfataricusAcid motifAcid sequenceSuch organismsMethanobacterium thermoautotrophicumLysRSProteinSynthetasesSynthetaseRNA synthetase
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
1995
Divergence of glutamate and glutamine aminoacylation pathways: Providing the evolutionary rationale for mischarging
Rogers K, Söll D. Divergence of glutamate and glutamine aminoacylation pathways: Providing the evolutionary rationale for mischarging. Journal Of Molecular Evolution 1995, 40: 476-481. PMID: 7783222, DOI: 10.1007/bf00166615.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseGlutamine tRNAEukaryotic organismsProkaryotic organismsGln-tRNAGlnHorizontal gene transfer eventsGene transfer eventsGlutaminyl-tRNA synthetasesGram-negative eubacteriaGlutamyl-tRNA synthetaseAminoacyl-tRNA synthetasesAminoacyl-tRNA synthetaseFamily of enzymesEukaryotic organellesPool of glutamateAminoacyl-tRNATRNADifferent cellular mechanismsEvolutionary rationaleProtein synthesisOrganismsAmino acidsTransfer eventsCellular mechanismsSynthetaseSubstrate 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
1993
Specificity in RNA: Protein Interactions; the Recognition of Escherichia Coli Glutamine tRNA
Rogers M, Weygand-Durašević I, Schwob E, Sherman J, Rogers K, Thomann H, Sylvers L, Jahn M, Inokuchi H, Ohtsuka E, Söll D. Specificity in RNA: Protein Interactions; the Recognition of Escherichia Coli Glutamine tRNA. 1993, 47-58. DOI: 10.1007/978-1-4615-2407-6_5.Peer-Reviewed Original ResearchProtein interactionsEscherichia coli glutaminyl-tRNA synthetaseRNA-protein structuresRole of tRNAGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetaseCognate aminoacyl-tRNA synthetaseRecognition of tRNAGenetic codeGlutamine tRNAAccuracy of translationRNA structureTRNABiophysical techniquesProtein synthesisMolecular levelMetabolic functionsAminoacyl-tRNA synthetase systemsCurrent understandingRNASynthetase systemSynthetaseUnusual elementsInteractionVariety
1991
Mutant enzymes and tRNAs as probes of the glutaminyl-tRNA synthetase: tRNAGln interaction
Enlisch-Peters S, Conley J, Plumbridge J, Leptak C, Söll D, Rogers M. Mutant enzymes and tRNAs as probes of the glutaminyl-tRNA synthetase: tRNAGln interaction. Biochimie 1991, 73: 1501-1508. PMID: 1725262, DOI: 10.1016/0300-9084(91)90184-3.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseEscherichia coli glutaminyl-tRNA synthetaseClass I aminoacyl-tRNA synthetaseTemperature-sensitive phenotypeAminoacyl-tRNA synthetaseTemperature-sensitive mutantGlutamine identityThree-dimensional structureMutant enzymesGlnRMutantsTerminal adenosineAminoacylation reactionExchange activitySynthetaseMutationsSubsequent assaysPseudorevertantsGlutaminylationTRNAAminoacylationGenesNucleotidesSpeciesColi
1990
Yeast suppressor mutations and transfer RNA processing
Nichols M, Willis I, Söll D. Yeast suppressor mutations and transfer RNA processing. Methods In Enzymology 1990, 181: 377-394. PMID: 2199758, DOI: 10.1016/0076-6879(90)81137-j.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBlotting, NorthernChromosomes, FungalGenes, FungalIndicators and ReagentsMolecular Sequence DataMutationNucleic Acid ConformationNucleic Acid HybridizationRNA Polymerase IIIRNA Processing, Post-TranscriptionalRNA, TransferRNA, Transfer, SerSaccharomyces cerevisiaeSuppression, GeneticTranscription FactorsTranscription, GeneticConceptsTRNA genesMature-sized tRNAsRNA processing reactionsPrimer-directed mutagenesisAminoacyl-tRNA synthetaseTransfer RNA moleculesCognate aminoacyl-tRNA synthetaseRNA processingSuppressor mutationsTRNA locusElongation factorProtein biosynthesisRibosomal interactionsRNA moleculesMutant strainStructural proteinsPink coloniesTranscription efficiencyProcessing reactionsProtein synthesisSuppressor functionTRNALow template concentrationsGenesLoci
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 formsSuppressorEscherichiaGlntRNA specificity of a mischarging aminoacyl‐tRNA synthetase: Glutamyl‐tRNA synthetase from barley chloroplasts
Schön A, Söll D. tRNA specificity of a mischarging aminoacyl‐tRNA synthetase: Glutamyl‐tRNA synthetase from barley chloroplasts. FEBS Letters 1988, 228: 241-244. DOI: 10.1016/0014-5793(88)80007-3.Peer-Reviewed Original Research
1985
[8] Glutaminyl-tRNA synthetase of Escherichia coli
Hoben P, Söll D. [8] Glutaminyl-tRNA synthetase of Escherichia coli. Methods In Enzymology 1985, 113: 55-59. PMID: 3911010, DOI: 10.1016/s0076-6879(85)13011-9.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseStructural geneSpecific aminoacyl-tRNA synthetaseE. coli chromosomeAmino acidsCognate amino acidTemperature-sensitive phenotypeGlutamyl-tRNA synthetaseAminoacyl-tRNA synthetaseColi chromosomeGln-tRNAGlnDNA fragmentsProtein synthesisEscherichia coliThermolabile enzymeCellular levelGenesGln mutationSynthetaseGlnRE. coliSeparate enzymesMultistep processNegative bacteriaEnzyme
1971
Enzymatic Modification of Transfer RNA
Söll D. Enzymatic Modification of Transfer RNA. Science 1971, 173: 293-299. PMID: 4934576, DOI: 10.1126/science.173.3994.293.Peer-Reviewed Original ResearchConceptsTRNA-modifying enzymesTRNA moleculesTRNA genesTransfer RNAAmino acid biosynthesisParticular tRNA speciesNucleic acid-protein interactionsAminoacyl-tRNA synthetaseSimple selection procedureAmino acid acceptorPrecursor tRNAsActive tRNAMature tRNACellular processesTRNA speciesRegulatory mutantsAcid biosynthesisRNA precursorsProtein factorsIsoacceptor tRNAsDifferent amino acidsNucleotide sequencePolynucleotide levelBiological functionsTRNA