2006
Saccharomyces cerevisiae imports the cytosolic pathway for Gln‐tRNA synthesis into the mitochondrion
Krett B, Rinehart J, Rubio M, Alfonzo J, Söll D. Saccharomyces cerevisiae imports the cytosolic pathway for Gln‐tRNA synthesis into the mitochondrion. The FASEB Journal 2006, 20: a500-a500. DOI: 10.1096/fasebj.20.4.a500-b.Peer-Reviewed Original ResearchTransamidation pathwayMitochondrial translationGln-tRNAOrganellar protein synthesisYeast mitochondrial DNAGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesAminoacyl-tRNA formationImport mechanismMitochondrial localizationMitochondrial DNAProtein biosynthesisMost bacteriaCytoplasmic componentsAlternate functionsCytosolic pathwayProtein synthesisAmino acidsEssential processMitochondriaTRNAPathwayEukaryotesGlnRArchaea
2003
Non-canonical Eukaryotic Glutaminyl- and Glutamyl-tRNA Synthetases Form Mitochondrial Aminoacyl-tRNA in Trypanosoma brucei *
Rinehart J, Horn EK, Wei D, Söll D, Schneider A. Non-canonical Eukaryotic Glutaminyl- and Glutamyl-tRNA Synthetases Form Mitochondrial Aminoacyl-tRNA in Trypanosoma brucei *. Journal Of Biological Chemistry 2003, 279: 1161-1166. PMID: 14563839, DOI: 10.1074/jbc.m310100200.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseGlutamyl-tRNA synthetaseT. bruceiGln-tRNATrypanosoma bruceiInsect stage T. bruceiT. brucei enzymeRespective gene productsAminoacyl-tRNA synthetasesGlutamyl-tRNA synthetase activitySynthetase activityTransamidation pathwayLeishmania mitochondriaBrucei enzymeMitochondrial tRNAsGlu-tRNAProtein biosynthesisAminoacylation experimentsGene productsRNA interferenceTRNABruceiMitochondriaTotal tRNAGlutaminyl
2000
A Mutant Escherichia coli Tyrosyl-tRNA Synthetase Utilizes the Unnatural Amino Acid Azatyrosine More Efficiently than Tyrosine*
Hamano-Takaku F, Iwama T, Saito-Yano S, Takaku K, Monden Y, Kitabatake M, Söll D, Nishimura S. A Mutant Escherichia coli Tyrosyl-tRNA Synthetase Utilizes the Unnatural Amino Acid Azatyrosine More Efficiently than Tyrosine*. Journal Of Biological Chemistry 2000, 275: 40324-40328. PMID: 11006270, DOI: 10.1074/jbc.m003696200.Peer-Reviewed Original ResearchConceptsUnnatural amino acidsTyrosyl-tRNA synthetaseEscherichia coli tyrosyl-tRNA synthetasePosition 130Amino acidsVivo protein biosynthesisE. coli cellsAminoacyl-tRNA formationSingle point mutationTyrRS mutantsCellular proteinsProtein biosynthesisTYR geneMutant enzymesPlasmid libraryReplacement of phenylalanineColi cellsImmense potentialNormal phenotypeEfficient productionPoint mutationsTyrRSProteinPolymerase chain reaction techniqueSynthetaseDomain-specific recruitment of amide amino acids for protein synthesis
Tumbula D, Becker H, Chang W, Söll D. Domain-specific recruitment of amide amino acids for protein synthesis. Nature 2000, 407: 106-110. PMID: 10993083, DOI: 10.1038/35024120.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseAsparaginyl-tRNA synthetaseProtein synthesisAmino acidsAminoacyl-transfer RNAAmino acid metabolismGlu-tRNAGlnAsn-tRNAProtein biosynthesisGln-tRNAArchaeaTRNASynthetaseAmidotransferaseBacteriaAmidotransferasesDirect evidenceDifferent mechanismsBiosynthesisCentral importanceCrucial stepRNAOrganismsDomainCytoplasm
1999
Archaeal Aminoacyl-tRNA Synthesis: Diversity Replaces Dogma
Tumbula D, Vothknecht U, Kim H, Ibba M, Min B, Li T, Pelaschier J, Stathopoulos C, Becker H, Söll D. Archaeal Aminoacyl-tRNA Synthesis: Diversity Replaces Dogma. Genetics 1999, 152: 1269-1276. PMID: 10430557, PMCID: PMC1460689, DOI: 10.1093/genetics/152.4.1269.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthesisGene transfer eventsPhenylalanyl-tRNA synthetasesLysyl-tRNA synthetaseTransamidation pathwayExtant organismsMethanococcus jannaschiiAsparaginyl-tRNAProtein biosynthesisGenetic codeGene expressionGenome sequencingAminoacyl-tRNAArchaeaMethanobacterium thermoautotrophicumMolecular biologyUnexpected levelNovel pathwayTransfer eventsFaithful translationPathwayJannaschiiSynthetasesBiosynthesisOrganisms
1997
Archaeal-type lysyl-tRNA synthetase in the Lyme disease spirochete Borrelia burgdorferi
Ibba M, Bono J, Rosa P, Söll D. Archaeal-type lysyl-tRNA synthetase in the Lyme disease spirochete Borrelia burgdorferi. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 14383-14388. PMID: 9405621, PMCID: PMC24988, DOI: 10.1073/pnas.94.26.14383.Peer-Reviewed Original ResearchConceptsLysyl-tRNA synthetasesLysyl-tRNA synthetaseOpen reading frameReading frameAminoacyl-tRNA synthetasesLyme disease spirochete Borrelia burgdorferiGroup of enzymesLysyl-tRNA synthetase activityAmino acid levelsBacterial pathogen Borrelia burgdorferiArchaeal kingdomHeterologous expressionProtein biosynthesisGenomic sequencesMRNA translationPathogen Borrelia burgdorferiSignificant similarityLysyl-tRNASynthetasesB. burgdorferiBorrelia burgdorferiEscherichia coliEukaryaSpirochete Borrelia burgdorferiPathogenic spirochetes
1996
Glutamyl-transfer RNA: at the crossroad between chlorophyll and protein biosynthesis
Kumar A, Schaub U, Söll D, Ujwal M. Glutamyl-transfer RNA: at the crossroad between chlorophyll and protein biosynthesis. Trends In Plant Science 1996, 1: 371-376. DOI: 10.1016/s1360-1385(96)80311-6.Peer-Reviewed Original ResearchTransfer RNAConversion of GSAGlu-tRNA reductaseEssential biosynthetic processesVariety of plantsChlorophyll biosynthesisGlu-tRNAHigher plantsProtein biosynthesisBiosynthetic processesBiosynthesisPlantsPivotal stepFirst pivotal stepChloroplastsKey precursorBiosynthesesGenesRNAProteinReductaseChlorophyllEnzymeRegulationAla
1994
Transfer RNA in Its Fourth Decade
RajBhandary U, Söll D. Transfer RNA in Its Fourth Decade. 1994, 1-4. DOI: 10.1128/9781555818333.ch1.Peer-Reviewed Original Research
1992
Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation
Sherman J, Rogers M, Söll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Research 1992, 20: 2847-2852. PMID: 1377381, PMCID: PMC336931, DOI: 10.1093/nar/20.11.2847.Peer-Reviewed Original ResearchConceptsAccuracy of aminoacylationAminoacyl-tRNA synthetasesTyrosyl-tRNA synthetaseE. coli tyrosyl-tRNA synthetaseEscherichia coli tyrosyl-tRNA synthetaseGlutaminyl-tRNA synthetaseLevel of aminoacylationProtein biosynthesisTRNASynthetasesAminoacylationCompetition assaysDiscriminator baseDifferent synthetasesConcurrent overexpressionCorrect aminoacylationSynthetaseFirst baseRelative affinityVivoMisacylationAssaysAnticodonBiosynthesisCompetitionCompetition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation
Sherman J, Rogers M, Söll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Research 1992, 20: 1547-1552. PMID: 16617497, PMCID: PMC312236, DOI: 10.1093/nar/20.7.1547.Peer-Reviewed Original ResearchAccuracy of aminoacylationAminoacyl-tRNA synthetasesTyrosyl-tRNA synthetaseE. coli tyrosyl-tRNA synthetaseEscherichia coli tyrosyl-tRNA synthetaseGlutaminyl-tRNA synthetaseLevel of aminoacylationProtein biosynthesisTRNASynthetasesAminoacylationCompetition assaysDiscriminator baseDifferent synthetasesConcurrent overexpressionCorrect aminoacylationSynthetaseFirst baseRelative affinityVivoMisacylationAssaysAnticodonBiosynthesisCompetition
1991
Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetase
Jahn M, Rogers M, Söll D. Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetase. Nature 1991, 352: 258-260. PMID: 1857423, DOI: 10.1038/352258a0.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseMutant tRNAsE. coli glutaminyl-tRNA synthetaseEfficient amber suppressorsAminoacyl-tRNA synthetasesCorresponding transfer RNASet of nucleotidesMajor recognition elementGlutamine identityAcceptor stem regionTRNA discriminationTransfer RNAAmber suppressorProtein biosynthesisTRNA moleculesUnmodified tRNACorrect attachmentAnticodon regionTRNAAcceptor stemSimilar kinetic parametersEscherichia coliAmino acidsDifferent synthetasesSpecificity constant
1990
The accuracy of aminoacylation — ensuring the fidelity of the genetic code
Söll D. The accuracy of aminoacylation — ensuring the fidelity of the genetic code. Cellular And Molecular Life Sciences 1990, 46: 1089-1096. PMID: 2253707, DOI: 10.1007/bf01936918.Peer-Reviewed Original ResearchConceptsAccuracy of aminoacylationTransfer RNA speciesAminoacyl-tRNA synthetasesMessenger RNA codonRNA speciesProtein biosynthesisGenetic codeProtein interactionsParticular tRNATRNACorrect attachmentBiophysical techniquesRNA codonsAmino acidsSynthetasesSpecific recognitionProper interactionAnticodonBiosynthesisCodonAminoacylationNucleotidesSpeciesEnzymeIdentity elementExpression of the Synechocystis sp. strain PCC 6803 tRNA(Glu) gene provides tRNA for protein and chlorophyll biosynthesis
O'Neill G, Söll D. Expression of the Synechocystis sp. strain PCC 6803 tRNA(Glu) gene provides tRNA for protein and chlorophyll biosynthesis. Journal Of Bacteriology 1990, 172: 6363-6371. PMID: 2121711, PMCID: PMC526821, DOI: 10.1128/jb.172.11.6363-6371.1990.Peer-Reviewed Original ResearchConceptsSynechocystis 6803Synechocystis spFirst anticodon baseStrain PCC 6803Cyanobacterium Synechocystis spTotal tRNA populationAmount of chlorophyllNorthern blot analysisChlorophyll biosynthesisALA biosynthesisPrecursor tRNAsPCC 6803TRNA speciesProtein biosynthesisTRNA populationCellular RNAAminoacylation assaysChlorophyll levelsBiosynthesisAddition of inhibitorsBlot analysisTranslation systemDelta-aminolevulinic acidTRNAChlorophyllYeast 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 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
1974
15. Aminoacyl-tRNA Synthetases
Söll D, Schimmel P. 15. Aminoacyl-tRNA Synthetases. The Enzymes 1974, 10: 489-538. DOI: 10.1016/s1874-6047(08)60147-x.Peer-Reviewed Original ResearchAminoacyl-tRNA synthetasesEucaryotic organismsSpecific aminoacyl-tRNA synthetasesCorresponding cytoplasmic enzymesFamily of enzymesMitochondrial tRNAsProtein biosynthesisMammalian cellsMammalian virusesSynthetasesCytoplasmic enzymeSeparate proteinsCell extractsTRNAAmino acidsOrganismsCytoplasmSame organismEnzymeOrganellesMitochondriaMachineryProteinKey roleProcaryotes
1969
CYTOKININS: DISTRIBUTION IN TRANSFER RNA SPECIES OF Escherichia coli*
Armstrong D, Burrows W, Skoog F, Roy K, Söll D. CYTOKININS: DISTRIBUTION IN TRANSFER RNA SPECIES OF Escherichia coli*. Proceedings Of The National Academy Of Sciences Of The United States Of America 1969, 63: 834-841. PMID: 4899879, PMCID: PMC223528, DOI: 10.1073/pnas.63.3.834.Peer-Reviewed Original Research