2023
Recoding UAG to selenocysteine in Saccharomyces cerevisiae
Hoffman K, Chung C, Mukai T, Krahn N, Jiang H, Balasuriya N, O'Donoghue P, Söll D. Recoding UAG to selenocysteine in Saccharomyces cerevisiae. RNA 2023, 29: 1400-1410. PMID: 37279998, PMCID: PMC10573291, DOI: 10.1261/rna.079658.123.Peer-Reviewed Original ResearchConceptsSelenoprotein productionYeast expression systemSeryl-tRNA synthetaseSite-specific incorporationEukaryotic relativesKingdom FungiSelenocysteine synthaseSelenophosphate synthetaseBiosynthesis pathwayEukaryotic selenoproteinsMetabolic engineeringBiosynthetic pathwayPathway componentsExpression systemReductase enzymeTRNASaccharomycesYeastTranslation componentsSpecific sitesFacile productionUnique chemicalSynthetasePathwayFirst demonstration
2011
An unusual tRNAThr derived from tRNAHis reassigns in yeast mitochondria the CUN codons to threonine
Su D, Lieberman A, Lang BF, Simonović M, Söll D, Ling J. An unusual tRNAThr derived from tRNAHis reassigns in yeast mitochondria the CUN codons to threonine. Nucleic Acids Research 2011, 39: 4866-4874. PMID: 21321019, PMCID: PMC3113583, DOI: 10.1093/nar/gkr073.Peer-Reviewed Original ResearchConceptsCUN codonsYeast mitochondriaGenetic codeAlloacceptor tRNA gene recruitmentComprehensive phylogenetic analysisStandard genetic codeThreonyl-tRNA synthetaseHistidyl-tRNA synthetaseGene recruitmentEvolutionary originPhylogenetic analysisRecoding eventBiochemical experimentsFirst nucleotideAnticodon loopMST1CodonFirst clear exampleYeastMitochondriaThreonineSynthetaseCandida albicansGenomeClear example
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
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
1993
Incomplete citric acid cycle obliges aminolevulinic acid synthesis via the C5 pathway in a methylotroph
Lloyd A, Weitzman P, Söll D. Incomplete citric acid cycle obliges aminolevulinic acid synthesis via the C5 pathway in a methylotroph. Microbiology 1993, 139: 2931-2938. DOI: 10.1099/00221287-139-12-2931.Peer-Reviewed Original ResearchC5 pathwayM. methylotrophusAminolevulinic acid synthesisTRNA-dependent mannerConversion of pyruvateCitric acid cycleMalate dehydrogenase activityMammalian cellsGlyoxylate cycleALA formationCell-free extractsGlu-tRNAGluAcid cycleIsocitrate dehydrogenaseMethylophilus methylotrophusCatabolic roleAcid synthesisPathwayEnzymic activityDehydrogenase activityEnzymeConnected pathwaysAlaMethylotrophsYeast
1990
Purification and characterization of Chlamydomonas reinhardtii chloroplast glutamyl-tRNA synthetase, a natural misacylating enzyme.
Chen M, Jahn D, Schön A, O'Neill G, Söll D. Purification and characterization of Chlamydomonas reinhardtii chloroplast glutamyl-tRNA synthetase, a natural misacylating enzyme. Journal Of Biological Chemistry 1990, 265: 4054-4057. PMID: 2303494, DOI: 10.1016/s0021-9258(19)39701-7.Peer-Reviewed Original ResearchConceptsGlutamyl-tRNA synthetaseChloroplast enzymeApparent molecular massSequential column chromatographyChlamydomonas reinhardtiiActive enzymeMolecular massNondenaturing conditionsEscherichia coliDenaturing conditionsAcceptor RNASynthetaseMono S.Mono QEnzymeTRNAReinhardtiiYeastColumn chromatographyRNACytoplasmicProteinBarleyColiReversed phase chromatographyEnzymatic addition of guanylate to histidine transfer RNA
Williams J, Cooley L, Söll D. Enzymatic addition of guanylate to histidine transfer RNA. Methods In Enzymology 1990, 181: 451-462. PMID: 2166216, DOI: 10.1016/0076-6879(90)81143-i.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell LineChromatography, AffinityChromatography, DEAE-CelluloseChromatography, Ion ExchangeDrosophilaElectrophoresis, Polyacrylamide GelGuanosine TriphosphateKineticsNucleotidyltransferasesPhosphorus RadioisotopesRadioisotope Dilution TechniqueRNA, Transfer, Amino Acid-SpecificRNA, Transfer, HisSaccharomyces cerevisiaeSubstrate SpecificityConceptsHistidine tRNATransfer RNABacteriophage T5Yeast enzymeEnzyme migratesUridine residuesExtra nucleotidesLigase mechanismAdditional nucleotidesEnzymatic additionGel filtration chromatographyEnzyme intermediateTRNAAbsolute requirementEnzymeMolecular weightNucleotidesUltrogel AcA 34Filtration chromatographyATPDrosophilaAcA 34Molecular weight markersYeastTitration experiments
1980
Dimeric tRNA precursors in yeast
Schmidt O, Mao J, Ogden R, Beckmann J, Sakano H, Abelson J, Söll D. Dimeric tRNA precursors in yeast. Nature 1980, 287: 750-752. PMID: 6253814, DOI: 10.1038/287750a0.Peer-Reviewed Original ResearchConceptsDimeric tRNA precursorTRNA precursorsDNA fragmentsYeast tRNA genesDifferent genomic regionsNucleotide sequence analysisTRNA genesSaccharomyces cerevisiae1Xenopus nucleiGenomic regionsSpecific transcriptionTRNA speciesPrecursor RNARNA precursorsTRNA moleculesGene regionSequence analysisGene configurationEnzyme activityGenesMode of expressionFragmentsTranscriptionYeastTRNAAsp
1971
Purification of Five Leucine Transfer Ribonucleic Acid Species from Escherichia coli and Their Acylation by Heterologous Leucyl-Transfer Ribonucleic Acid Synthetase
Blank H, Söll D. Purification of Five Leucine Transfer Ribonucleic Acid Species from Escherichia coli and Their Acylation by Heterologous Leucyl-Transfer Ribonucleic Acid Synthetase. Journal Of Biological Chemistry 1971, 246: 4947-4950. PMID: 4936719, DOI: 10.1016/s0021-9258(18)61954-4.Peer-Reviewed Original ResearchMeSH KeywordsAcylationBase SequenceBenzoatesCarbon IsotopesCarcinomaCell LineChromatography, DEAE-CelluloseChromatography, GelDrug StabilityEscherichia coliGenetic CodeHot TemperatureKineticsLeucineLigasesMouth NeoplasmsNucleic Acid DenaturationPolynucleotidesRibosomesRNA, BacterialRNA, TransferTemplates, GeneticYeasts
1970
Purification of Five Serine Transfer Ribonucleic Acid Species from Escherichia coli and Their Acylation by Homologous and Heterologous Seryl Transfer Ribonucleic Acid Synthetases
Roy K, Söll D. Purification of Five Serine Transfer Ribonucleic Acid Species from Escherichia coli and Their Acylation by Homologous and Heterologous Seryl Transfer Ribonucleic Acid Synthetases. Journal Of Biological Chemistry 1970, 245: 1394-1400. PMID: 4910052, DOI: 10.1016/s0021-9258(18)63249-1.Peer-Reviewed Original Research
1967
Studies on polynucleotides LXXV. Specificity of tRNA for codon recognition as studied by the ribosomal binding technique
Söll D, Cherayil J, Bock R. Studies on polynucleotides LXXV. Specificity of tRNA for codon recognition as studied by the ribosomal binding technique. Journal Of Molecular Biology 1967, 29: 97-112. PMID: 4861614, DOI: 10.1016/0022-2836(67)90183-0.Peer-Reviewed Original ResearchConceptsTransfer RNAAmino acidsE. coliIndividual amino acidsCodon recognitionMultiple codonsMultiple speciesRespective amino acidsWobble hypothesisYeast transfer RNAEscherichia coliCodonRNAColiYeastSpeciesBindingRecognition patternsTRNARibosomesThird letterStimulation of bindingTrinucleotideAcidInteresting differences
1966
Specificity of sRNA for recognition of codons as studied by the ribosomal binding technique
Söll D, Jones D, Ohtsuka E, Faulkner R, Lohrmann R, Hayatsu H, Khorana H, Cherayil J, Hampel A, Bock R. Specificity of sRNA for recognition of codons as studied by the ribosomal binding technique. Journal Of Molecular Biology 1966, 19: 556-573. PMID: 5338858, DOI: 10.1016/s0022-2836(66)80023-2.Peer-Reviewed Original Research