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
1991
Mutant enzymes and tRNAs as probes of the glutaminyl-tRNA synthetase: tRNAGln interaction
Enlisch-Peters S, Conley J, Plumbridge J, Leptak C, Söll D, Rogers M. Mutant enzymes and tRNAs as probes of the glutaminyl-tRNA synthetase: tRNAGln interaction. Biochimie 1991, 73: 1501-1508. PMID: 1725262, DOI: 10.1016/0300-9084(91)90184-3.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseEscherichia coli glutaminyl-tRNA synthetaseClass I aminoacyl-tRNA synthetaseTemperature-sensitive phenotypeAminoacyl-tRNA synthetaseTemperature-sensitive mutantGlutamine identityThree-dimensional structureMutant enzymesGlnRMutantsTerminal adenosineAminoacylation reactionExchange activitySynthetaseMutationsSubsequent assaysPseudorevertantsGlutaminylationTRNAAminoacylationGenesNucleotidesSpeciesColi
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 elementEnzymatic 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
1988
Discrimination between glutaminyl-tRNA synthetase and seryl-tRNA synthetase involves nucleotides in the acceptor helix of tRNA.
Rogers M, Söll D. Discrimination between glutaminyl-tRNA synthetase and seryl-tRNA synthetase involves nucleotides in the acceptor helix of tRNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 6627-6631. PMID: 3045821, PMCID: PMC282030, DOI: 10.1073/pnas.85.18.6627.Peer-Reviewed Original Research
1982
Post-transcriptional nucleotide addition is responsible for the formation of the 5' terminus of histidine tRNA.
Cooley L, Appel B, Söll D. Post-transcriptional nucleotide addition is responsible for the formation of the 5' terminus of histidine tRNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1982, 79: 6475-6479. PMID: 6292903, PMCID: PMC347149, DOI: 10.1073/pnas.79.21.6475.Peer-Reviewed Original ResearchConceptsMature tRNAHistidine tRNAPrimary transcriptHistidine tRNA genesGuanylate residuePost-transcriptional additionDrosophila Kc cellsTRNA genesDrosophila melanogasterSchizosaccharomyces pombeTRNAs resultsRNA speciesRNase PEukaryotic mRNAsKc cellsRNA precursorsTRNASequence analysisNucleotide additionAdditional nucleotidesPhosphodiester bondGenesNucleotidesMaturation schemeTranscripts18 RNA Methylation
Söll D, Kline L. 18 RNA Methylation. The Enzymes 1982, 15: 557-566. DOI: 10.1016/s1874-6047(08)60290-5.Peer-Reviewed Original ResearchRNA methylationSpecific methyltransferase enzymesPost-transcriptional modificationsMethylation of tRNARNA methyltransferasesTRNA methyltransferaseBiological regulationSubstrate RNAHomologous RNAMethyltransferase enzymeTRNAMethylationS-adenosylmethionineMethyl donorMethyl-deficient tRNARNAE. coliMutantsMethyltransferaseEnzymeMethyltransferasesRRNANucleotidesIsolationColi19 Nucleotide Modification in RNA
Kline L, Söll D. 19 Nucleotide Modification in RNA. The Enzymes 1982, 15: 567-582. DOI: 10.1016/s1874-6047(08)60291-7.Peer-Reviewed Original ResearchRNA base modificationsAnticodon of tRNAComplex nucleotidesNucleotide modificationsAdenosine modificationsEnzymatic modificationRNA chainsBase modificationsEnzymatic stepsAdenosine residuesUracil residuesNucleotidesRNABiochemical evidenceEnzymeModifying groupUracil nucleotidesResiduesGuanine structureFirst positionTRNAAnticodonGeneticsTranscriptsModificationGenes for tRNA 5Lys from Drosophila melanogaster
DeFranco D, Burke K, Hayashi S, Tener G, Miller R, Söll D. Genes for tRNA 5Lys from Drosophila melanogaster. Nucleic Acids Research 1982, 10: 5799-5808. PMID: 6292853, PMCID: PMC320931, DOI: 10.1093/nar/10.19.5799.Peer-Reviewed Original Research
1981
Identification of regulatory sequences contained in the 5'-flanking region of Drosophila lysine tRNA2 genes.
DeFranco D, Sharp S, Söll D. Identification of regulatory sequences contained in the 5'-flanking region of Drosophila lysine tRNA2 genes. Journal Of Biological Chemistry 1981, 256: 12424-12429. PMID: 6913581, DOI: 10.1016/s0021-9258(18)43290-5.Peer-Reviewed Original ResearchConceptsTRNA genesTranscriptional repressionMature tRNATemplate activityDrosophila tRNA genesLow template activityInsertion of nucleotidesPoor transcriptional activityRegulatory sequencesDeletion analysisNucleotides 23Transcriptional activityAdditional nucleotidesGenesTRNARepressionNucleotidesTranscriptionComplete lossSequenceDeletionOligonucleotideOligonucleotide sequencesRegionActivity
1979
The nucleotide sequence of a cloned Drosophila arginine tRNA gene and its in vitro transcription in Xenopus germinal vesicle extracts.
Silverman S, Schmidt O, Söll D, Hovemann B. The nucleotide sequence of a cloned Drosophila arginine tRNA gene and its in vitro transcription in Xenopus germinal vesicle extracts. Journal Of Biological Chemistry 1979, 254: 10290-10294. PMID: 114522, DOI: 10.1016/s0021-9258(19)86707-8.Peer-Reviewed Original ResearchConceptsMature tRNAPrecursor RNANucleotide sequenceDrosophila tRNAArg geneGerminal vesicle extractsArginine tRNA geneXenopus germinal vesicleTRNA genesTRNAArg genePrimary transcriptDNA sequencesLeader sequenceVesicle extractsT residuesGenesTranscriptionGerminal vesicleTerminusVitro systemTRNAA sequenceRNASequenceNucleotidesTRNAArgThe nucleotide sequence of lysine tRNA 2 from Drosophila
Silverman S, Gillam I, Tener G, Söll D. The nucleotide sequence of lysine tRNA 2 from Drosophila. Nucleic Acids Research 1979, 6: 435-442. PMID: 106371, PMCID: PMC327705, DOI: 10.1093/nar/6.2.435.Peer-Reviewed Original Research
1974
New aspects in tRNA biosynthesis
Schäfer K, Söll D. New aspects in tRNA biosynthesis. Biochimie 1974, 56: 795-804. PMID: 4614860, DOI: 10.1016/s0300-9084(74)80500-6.Peer-Reviewed Original Research
1973
Nucleotide Modification In Vitro of the Precursor of Transfer RNATyr of Escherichia coli
Schaefer K, Altman S, Söll D. Nucleotide Modification In Vitro of the Precursor of Transfer RNATyr of Escherichia coli. Proceedings Of The National Academy Of Sciences Of The United States Of America 1973, 70: 3626-3630. PMID: 4587257, PMCID: PMC427294, DOI: 10.1073/pnas.70.12.3626.Peer-Reviewed Original Research
1971
The nucleotide sequence of two leucine tRNA species from Escherichia coli K12
Blank H, Sőll D. The nucleotide sequence of two leucine tRNA species from Escherichia coli K12. Biochemical And Biophysical Research Communications 1971, 43: 1192-1197. PMID: 4936129, DOI: 10.1016/0006-291x(71)90589-4.Peer-Reviewed Original Research