2001
A Single Amidotransferase Forms Asparaginyl-tRNA and Glutaminyl-tRNA in Chlamydia trachomatis *
Raczniak G, Becker H, Min B, Söll D. A Single Amidotransferase Forms Asparaginyl-tRNA and Glutaminyl-tRNA in Chlamydia trachomatis *. Journal Of Biological Chemistry 2001, 276: 45862-45867. PMID: 11585842, DOI: 10.1074/jbc.m109494200.Peer-Reviewed Original ResearchConceptsAsn-tRNAGln-tRNAAminoacyl-tRNAOperon-like arrangementAccurate protein synthesisGlutaminyl-tRNA synthetaseGlutamyl-tRNA synthetaseAminoacyl-tRNA synthetasesAsparaginyl-tRNA synthetaseAspartyl-tRNA synthetaseGat genesAsparaginyl-tRNAGenome sequenceMost bacteriaGlutaminyl-tRNAAmidotransferaseProtein synthesisSynthetasesSynthetaseGenesAmide donorEnzymeAspGluGenome
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 techniqueSynthetaseThe 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
1999
Cysteinyl‐tRNA formation: the last puzzle of aminoacyl‐tRNA synthesis
Li T, Graham D, Stathopoulos C, Haney P, Kim H, Vothknecht U, Kitabatake M, Hong K, Eggertsson G, Curnow A, Lin W, Celic I, Whitman W, Söll D. Cysteinyl‐tRNA formation: the last puzzle of aminoacyl‐tRNA synthesis. FEBS Letters 1999, 462: 302-306. PMID: 10622715, DOI: 10.1016/s0014-5793(99)01550-1.Peer-Reviewed Original ResearchConceptsLateral gene transferAminoacyl-tRNA synthesisCysteinyl-tRNA synthetaseEscherichia coli cysteinyl-tRNA synthetaseMolecular phylogenyPyrococcus sppMethanococcus jannaschiiMethanococcus maripaludisM. maripaludisMethanogenic archaeaMethanosarcina sppGene transferCysRSMethanosarcina barkeriGenesSpecific relativeLast puzzleSppOrthologsArchaeaPhylogenyJannaschiiMutantsLineagesOrganismsSubstrate recognition by class I lysyl-tRNA synthetases: A molecular basis for gene displacement
Ibba M, Losey H, Kawarabayasi Y, Kikuchi H, Bunjun S, Söll D. Substrate recognition by class I lysyl-tRNA synthetases: A molecular basis for gene displacement. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 418-423. PMID: 9892648, PMCID: PMC15151, DOI: 10.1073/pnas.96.2.418.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesBase SequenceBorrelia burgdorferi GroupCloning, MolecularDiphosphatesEscherichia coliEvolution, MolecularGenes, ArchaealGenes, BacterialGenetic Complementation TestKineticsLysine-tRNA LigaseMethanococcusMolecular Sequence DataNucleic Acid ConformationPhylogenyRNA, Transfer, Amino AcylSequence Analysis, DNASubstrate SpecificityTranscription, GeneticConceptsClass II LysRSAminoacyl-tRNA synthetasesLysyl-tRNA synthetasesSubstrate recognitionMolecular basisBacterial class IClass II enzymesSequence-specific recognitionGene displacementTranslational apparatusTRNA recognitionEscherichia coli strainsLysRSLysRSsSame nucleotideSynthetasesDiscriminator baseUnrelated typesLysine activationCertain bacteriaII enzymesColi strainsTRNALysClass IEnzyme
1998
Major Identity Element of Glutamine tRNAs from Bacillus subtilis and Escherichia coli in the Reaction with B. subtilis Glutamyl-tRNA Synthetase
Kim S, Söll D. Major Identity Element of Glutamine tRNAs from Bacillus subtilis and Escherichia coli in the Reaction with B. subtilis Glutamyl-tRNA Synthetase. Molecules And Cells 1998, 8: 459-465. PMID: 9749534, DOI: 10.1016/s1016-8478(23)13451-0.Peer-Reviewed Original Research
1997
A nuclear genetic lesion affecting Saccharomyces cerevisiae mitochondrial translation is complemented by a homologous Bacillus gene
Kim S, Stange-Thomann N, Martins O, Hong K, Söll D, Fox T. A nuclear genetic lesion affecting Saccharomyces cerevisiae mitochondrial translation is complemented by a homologous Bacillus gene. Journal Of Bacteriology 1997, 179: 5625-5627. PMID: 9287027, PMCID: PMC179443, DOI: 10.1128/jb.179.17.5625-5627.1997.Peer-Reviewed Original ResearchMeSH KeywordsBacillus subtilisDNA, FungalDNA, MitochondrialFungal ProteinsGenes, BacterialMitochondrial ProteinsMolecular Sequence DataProtein BiosynthesisRecombinant Fusion ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSequence Analysis, DNASequence Homology, Amino AcidTransaminasesTranscription Factors
1996
Lactobacillus bulgaricus asparagine synthetase and asparaginyl-tRNA synthetase: coregulation by transcription antitermination?
Kim S, Germond J, Pridmore D, Söll D. Lactobacillus bulgaricus asparagine synthetase and asparaginyl-tRNA synthetase: coregulation by transcription antitermination? Journal Of Bacteriology 1996, 178: 2459-2461. PMID: 8636057, PMCID: PMC177964, DOI: 10.1128/jb.178.8.2459-2461.1996.Peer-Reviewed Original ResearchAmino Acid SequenceAmino Acyl-tRNA SynthetasesAspartate-Ammonia LigaseAspartate-tRNA LigaseBase SequenceGene Expression Regulation, BacterialGenes, BacterialGenetic Complementation TestLactobacillusMolecular Sequence DataNucleic Acid ConformationRNA, Transfer, Amino AcylSequence Homology, Amino AcidTerminator Regions, GeneticTranscription, GeneticHomologous Expression and Purification of Mutants of an Essential Protein by Reverse Epitope-Tagging
Thomann H, Ibba M, Hong K, Söll D. Homologous Expression and Purification of Mutants of an Essential Protein by Reverse Epitope-Tagging. Bio/Technology 1996, 14: 50-55. PMID: 9636312, DOI: 10.1038/nbt0196-50.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseMutant enzymesEssential enzymeGlutaminyl-tRNA synthetasesWild-type proteinExtrachromosomal genetic elementsEpitope taggingEssential proteinsMutant proteinsHomologous expressionReporter epitopeCell-free extractsGenetic elementsNormal phenotypeBiochemical studiesEnzymatic activityEnzymeProteinSynthetaseProtein contaminationExpressionPurificationMutantsSynthetasesNovel strategyEscherichia coli Tryptophanyl-tRNA Synthetase Mutants Selected for Tryptophan Auxotrophy Implicate the Dimer Interface in Optimizing Amino Acid Binding †
Sever S, Rogers K, Rogers M, Carter C, Söll D. Escherichia coli Tryptophanyl-tRNA Synthetase Mutants Selected for Tryptophan Auxotrophy Implicate the Dimer Interface in Optimizing Amino Acid Binding †. Biochemistry 1996, 35: 32-40. PMID: 8555191, DOI: 10.1021/bi952103d.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacillus subtilisBase SequenceBinding SitesCloning, MolecularDNA PrimersEscherichia coliGenes, BacterialGeobacillus stearothermophilusHaemophilus influenzaeKineticsMacromolecular SubstancesModels, MolecularMolecular Sequence DataPolymerase Chain ReactionProtein FoldingProtein Structure, SecondaryRecombinant ProteinsRestriction MappingSequence Homology, Amino AcidTryptophanTryptophan-tRNA LigaseConceptsTryptophanyl-tRNA synthetaseDimer interfaceClass I aminoacyl-tRNA synthetasesAminoacyl-tRNA synthetasesAmino acid bindingAmino acid activationActive siteSteady-state kinetic analysisSynthetase mutantsRossmann foldApparent KmKMSKS loopTrp lociProtein structureTrpR proteinTryptophan auxotrophDimeric enzymeAuxotrophic strainsBacillus stearothermophilusAcid bindingEscherichia coliOptimal catalysisAminoacyl adenylatesMutantsMutations
1994
Thiobacillus ferrooxidans tyrosyl-tRNA synthetase functions in vivo in Escherichia coli
Salazar O, Sagredo B, Jedlicki E, Söll D, Weygand-Durasevic I, Orellana O. Thiobacillus ferrooxidans tyrosyl-tRNA synthetase functions in vivo in Escherichia coli. Journal Of Bacteriology 1994, 176: 4409-4415. PMID: 7517395, PMCID: PMC205654, DOI: 10.1128/jb.176.14.4409-4415.1994.Peer-Reviewed Original ResearchMeSH KeywordsAcidithiobacillus thiooxidansAmino Acid SequenceBase SequenceGene Expression Regulation, BacterialGenes, BacterialGenetic Complementation TestMolecular Sequence DataMutationNucleic Acid HybridizationOperonPromoter Regions, GeneticRNA, BacterialRNA, RibosomalRNA, Transfer, TyrSequence Analysis, DNATyrosine-tRNA LigaseConceptsOverall identityTyrosyl-tRNA synthetase geneRho-independent transcription terminatorEscherichia coli TyrRSClass I aminoacyl-tRNA synthetasesRibosomal RNA operonSingle-copy geneAminoacyl-tRNA synthetasesTyrosyl-tRNA synthetasesSouthern blot analysisRNA operonBioleaching of mineralsThermosensitive mutationTranscription unitTranscription terminatorSynthetase genePutative promoterProtein sequencesSynthetase functionE. coli strainsGenesSignature sequencesEscherichia coliAmino acidsDNA probes
1992
Organization and nucleotide sequence of the glutamine synthetase (glnA) gene from Lactobacillus delbrueckii subsp. bulgaricus
Ishino Y, Morgenthaler P, Hottinger H, Söll D. Organization and nucleotide sequence of the glutamine synthetase (glnA) gene from Lactobacillus delbrueckii subsp. bulgaricus. Applied And Environmental Microbiology 1992, 58: 3165-3169. PMID: 1359838, PMCID: PMC183065, DOI: 10.1128/aem.58.9.3165-3169.1992.Peer-Reviewed Original ResearchConceptsOpen reading frameGlnA geneReading frameGlnA gene expressionGlutamine synthetase geneL. delbrueckii subspDNA sequence analysisMaxicell methodLactobacillus delbrueckii subspDelbrueckii subspGlnR geneDeletion strainNegative eubacteriaPositive eubacteriaSynthetase geneExtensive homologyRepressor geneNucleotide sequencePresent upstreamGene expressionBamHI fragmentUnknown functionSequence analysisClostridium acetobutylicumGenesSwitching tRNA(Gln) identity from glutamine to tryptophan.
Rogers M, Adachi T, Inokuchi H, Söll D. Switching tRNA(Gln) identity from glutamine to tryptophan. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 3463-3467. PMID: 1565639, PMCID: PMC48888, DOI: 10.1073/pnas.89.8.3463.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesAnticodonBase SequenceBeta-GalactosidaseCloning, MolecularEscherichia coliGenes, BacterialGenes, SuppressorGenes, SyntheticGlutamineMolecular Sequence DataMutagenesis, Site-DirectedNucleic Acid ConformationRNA, Transfer, GlnSuppression, GeneticTetrahydrofolate DehydrogenaseTryptophanConceptsOpal suppressorEscherichia coli glutaminyl-tRNA synthetaseAccuracy of aminoacylationGlutaminyl-tRNA synthetaseN-terminal sequence analysisEfficient suppressorYeast mitochondriaRespective tRNAsUCA anticodonAmber suppressorFol geneUGA codonUGA mutationsSequence analysisAlanine insertionAnticodonGenetic selectionBase pairsBase substitutionsSuppressorTRNATrpRSDihydrofolate reductasePosition 35MutationsGlutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression.
Verkamp E, Jahn M, Jahn D, Kumar A, Söll D. Glutamyl-tRNA reductase from Escherichia coli and Synechocystis 6803. Gene structure and expression. Journal Of Biological Chemistry 1992, 267: 8275-8280. PMID: 1569081, DOI: 10.1016/s0021-9258(18)42438-6.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde OxidoreductasesAmino Acid SequenceBase SequenceChromatography, GelCyanobacteriaEscherichia coliGene ExpressionGenes, BacterialGenes, FungalGenetic Complementation TestMolecular Sequence DataOpen Reading FramesPlasmidsRestriction MappingSaccharomyces cerevisiaeSequence Homology, Nucleic AcidConceptsGlutamyl-tRNA reductaseHemA geneAmino acid sequenceHemA proteinGluTR activitySynechocystis 6803Acid sequenceE. coliGlutamate-1-semialdehyde aminotransferaseHemA gene productEscherichia coliCyanobacterium Synechocystis spOpen reading frameEnterobacterium Escherichia coliDNA sequence analysisFunctional complementationGene structureGlu-tRNAGel filtration experimentsPCC 6803Synechocystis spGlutamyl-tRNAAcid polypeptideReading frameALA formation
1991
delta-Aminolevulinic acid dehydratase deficiency can cause delta-aminolevulinate auxotrophy in Escherichia coli
O'Neill G, Thorbjarnardóttir S, Michelsen U, Pálsson S, Söll D, Eggertsson G. delta-Aminolevulinic acid dehydratase deficiency can cause delta-aminolevulinate auxotrophy in Escherichia coli. Journal Of Bacteriology 1991, 173: 94-100. PMID: 1987138, PMCID: PMC207161, DOI: 10.1128/jb.173.1.94-100.1991.Peer-Reviewed Original ResearchConceptsALA dehydratase activityEscherichia coliWild-type geneClasses of mutantsDNA sequence analysisAminoglycoside antibiotic kanamycinHeme biosynthetic pathwayALA biosynthesisWild-type DNAAuxotrophic phenotypeComplementation studiesDehydratase activityHemB geneBiosynthetic pathwayPositive regulationALA formationSame geneMutantsPenicillin enrichmentSequence analysisGenesAntibiotic kanamycinDiffusible productHemB mutantEnzymatic activity
1989
The selenocysteine-inserting opal suppressor serine tRNA from E.coli is highly unusual in structure and modification
Schön A, Böck A, Ott G, Sprinzl M, Söll D. The selenocysteine-inserting opal suppressor serine tRNA from E.coli is highly unusual in structure and modification. Nucleic Acids Research 1989, 17: 7159-7165. PMID: 2529478, PMCID: PMC334795, DOI: 10.1093/nar/17.18.7159.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesBase SequenceChromatography, High Pressure LiquidCodonCysteineEscherichia coliGenes, BacterialMolecular Sequence DataNucleic Acid ConformationRNA, Transfer, Amino Acid-SpecificRNA, Transfer, SerSeleniumSelenocysteineStructure-Activity RelationshipSuppression, GeneticCharacterization of cis-acting mutations which increase expression of a glnS-lacZ fusion in Escherichia coli
Plumbridge J, Söll D. Characterization of cis-acting mutations which increase expression of a glnS-lacZ fusion in Escherichia coli. Molecular Genetics And Genomics 1989, 216: 113-119. PMID: 2471922, DOI: 10.1007/bf00332238.Peer-Reviewed Original Research
1988
The unusually long amino acid acceptor stem of Escherichia coli selenocysteine tRNA results from abnormal cleavage by RNase P
Burkard U, Söll D. The unusually long amino acid acceptor stem of Escherichia coli selenocysteine tRNA results from abnormal cleavage by RNase P. Nucleic Acids Research 1988, 16: 11617-11624. PMID: 3062578, PMCID: PMC339093, DOI: 10.1093/nar/16.24.11617.Peer-Reviewed Original ResearchEscherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity.
Uemura H, Conley J, Yamao F, Rogers J, Söll D. Escherichia coli glutaminyl-tRNA synthetase: a single amino acid replacement relaxes rRNA specificity. Protein Sequences And Data Analysis 1988, 1: 479-85. PMID: 2464170.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseTRNA bindingEscherichia coli glutaminyl-tRNA synthetaseExtensive homology searchesSingle amino acid replacementSingle amino acid changeRegion of homologyAminoacyl-tRNA synthetasesAmino acid replacementsAminoacyl adenylate formationAmino acids 235Amino acid changesLittle apparent similarityGlnS geneTRNA discriminationHomology searchGene productsAcid replacementsShare regionsDifferent tRNAsShort stretchesGenetic selectionAcid changesAsn changeHomology
1987
Allele-specific complementation of an Escherichia coli leuB mutation by a Lactobacillus bulgaricus tRNA gene
Hottinger H, Ohgi T, Zwahlen M, Dhamija S, Söll D. Allele-specific complementation of an Escherichia coli leuB mutation by a Lactobacillus bulgaricus tRNA gene. Gene 1987, 60: 75-83. PMID: 3326787, DOI: 10.1016/0378-1119(87)90215-0.Peer-Reviewed Original ResearchConceptsTRNA genesCopy numberWild-type formE. coli promotersHigh copy numberGene copy numberLeuB mutationClone bankLeucine prototrophyLow copy numberMissense suppressionNucleotide sequenceSerine tRNATerminator elementsGenesRestoration of activityTRNAEscherichia coliAmino acidsGene allelesExtra armE. coli