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
Synthetase competition and tRNA context determine the in vivo identity of tRNA discriminator mutants
Sherman J, Rogers K, Rogers M, Söll D. Synthetase competition and tRNA context determine the in vivo identity of tRNA discriminator mutants. Journal Of Molecular Biology 1992, 228: 1055-1062. PMID: 1474577, DOI: 10.1016/0022-2836(92)90314-a.Peer-Reviewed Original ResearchConceptsAmber suppressorTyrosine tRNAN-terminal protein sequencingGlutamyl-tRNA synthetaseE. coli dihydrofolate reductaseAminoacyl-tRNA synthetasesEffects of mutationsEfficiency of aminoacylationColi dihydrofolate reductaseSite of aminoacylationTyrosine specificityTRNAs exhibitGlutamine tRNAMutagenic analysisProtein sequencingGlutamate tRNAImportant identity elementVivo identityTRNANucleotide substitutionsTRNA identityDiscriminator baseDihydrofolate reductaseMultiple mutationsSynthetasesCompetition 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 affinityVivoMisacylationAssaysAnticodonBiosynthesisCompetition
1989
Structural Basis for Misaminoacylation by Mutant E. coli Glutaminyl-tRNA Synthetase Enzymes
Perona J, Swanson R, Rould M, Steitz T, Söll D. Structural Basis for Misaminoacylation by Mutant E. coli Glutaminyl-tRNA Synthetase Enzymes. Science 1989, 246: 1152-1154. PMID: 2686030, DOI: 10.1126/science.2686030.Peer-Reviewed Original Research