2001
A dual‐specific Glu‐tRNAGln and Asp‐tRNAAsn amidotransferase is involved in decoding glutamine and asparagine codons in Acidithiobacillus ferrooxidans
Salazar J, Zúñiga R, Raczniak G, Becker H, Söll D, Orellana O. A dual‐specific Glu‐tRNAGln and Asp‐tRNAAsn amidotransferase is involved in decoding glutamine and asparagine codons in Acidithiobacillus ferrooxidans. FEBS Letters 2001, 500: 129-131. PMID: 11445070, DOI: 10.1016/s0014-5793(01)02600-x.Peer-Reviewed Original ResearchConceptsOperon-like structureGlutaminyl-tRNA synthetaseGlutamyl-tRNA synthetaseA. ferrooxidansAsparaginyl-tRNA synthetaseTransamidation pathwayGat genesGlu-tRNAGlnBioleaching of mineralsAsn-tRNAAcidithiobacillus ferrooxidansGln-tRNAAsparagine codonsSynthetase enzymeBacillus subtilisAcidophilic bacteriumEscherichia coliBiochemical analysisAmidotransferaseSynthetaseGenes
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, Genetic
1995
A broadly applicable continuous spectrophotometric assay for measuring aminoacyl-tRNA synthetase activity
Lloyd A, Thomann H, Ibba M, Soöll D. A broadly applicable continuous spectrophotometric assay for measuring aminoacyl-tRNA synthetase activity. Nucleic Acids Research 1995, 23: 2886-2892. PMID: 7659511, PMCID: PMC307126, DOI: 10.1093/nar/23.15.2886.Peer-Reviewed Original Research
1994
Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases.
Frugier M, Söll D, Giegé R, Florentz C. Identity switches between tRNAs aminoacylated by class I glutaminyl- and class II aspartyl-tRNA synthetases. Biochemistry 1994, 33: 9912-21. PMID: 8060999, DOI: 10.1021/bi00199a013.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthetasesIdentity nucleotidesHigh-resolution X-ray structuresAminoacyl-tRNA synthetase complexGlutaminyl-tRNA synthetaseAspartyl-tRNA synthetasesAspartyl-tRNA synthetaseGlutamine identityCognate tRNATRNA structureTRNA moleculesTRNAAminoacylation specificitySynthetase complexSpecific aminoacylationConformational changesSynthetasesEscherichia coliYeastSynthetaseNucleotidesE. coliX-ray structureComplex formationColi
1988
Genomic organization of tRNA and aminoacyl-tRNA synthetase genes for two amino acids in Saccharomyces cerevisiae
Kolman C, Snyder M, Söll D. Genomic organization of tRNA and aminoacyl-tRNA synthetase genes for two amino acids in Saccharomyces cerevisiae. Genomics 1988, 3: 201-206. PMID: 3066745, DOI: 10.1016/0888-7543(88)90080-8.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthetase genesContour-clamped homogeneous electric field gel electrophoresisHomogeneous electric field gel electrophoresisSynthetase geneGenomic organizationSmall multigene familyDNA gel blotsAmino acidsField gel electrophoresisGel electrophoresisTRNA genesChromosome assignmentMultigene familyGel blotsGene sequencesS. cerevisiaeChromosomal DNATRNAGenesSaccharomycesAspartic acidElectrophoresisGenomeCerevisiaeFamily