2000
The 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
1998
Maize mitochondrial seryl-tRNA synthetase recognizes Escherichia coli tRNASer in vivo and in vitro
Rokov J, Söll D, Weygand-Durašević I. Maize mitochondrial seryl-tRNA synthetase recognizes Escherichia coli tRNASer in vivo and in vitro. Plant Molecular Biology 1998, 38: 497-502. PMID: 9747857, DOI: 10.1023/a:1006088516228.Peer-Reviewed Original ResearchConceptsSeryl-tRNA synthetaseMitochondrial seryl-tRNA synthetasePutative mature proteinSeryl-tRNA synthetasesEscherichia coliStructure/function relationshipsMature proteinGene sequencesMutant strainSignificant similarityFunctional identityN-terminalYeast tRNAMitochondrial functionFunction relationshipsProteinPoor substrateSynthetaseColiSynthetasesTRNAVivoCDNAMaizeEnzyme
1995
Aminoacylation of transfer RNAs with 2-thiouridine derivatives in the wobble position of the anticodon
Rogers K, Crescenzo A, Söll D. Aminoacylation of transfer RNAs with 2-thiouridine derivatives in the wobble position of the anticodon. Biochimie 1995, 77: 66-74. PMID: 7541255, DOI: 10.1016/0300-9084(96)88106-5.Peer-Reviewed Original ResearchConceptsEvolution of specificityPost-transcriptional modificationsAnticodon of tRNAAminoacyl-tRNA synthetasesTranslational regulationTransfer RNAWobble positionWobble baseLysine tRNATRNAEscherichia coliAnticodonAminoacylationFirst positionSynthetasesRNAColiRegulationGlutamineModificationDiscoveryGlutamate
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 formationColiCoexpression of eukaryotic tRNASer and yeast seryl-tRNA synthetase leads to functional amber suppression in Escherichia coli
Weygand-Durasević I, Nalaskowska M, Söll D. Coexpression of eukaryotic tRNASer and yeast seryl-tRNA synthetase leads to functional amber suppression in Escherichia coli. Journal Of Bacteriology 1994, 176: 232-239. PMID: 8282701, PMCID: PMC205035, DOI: 10.1128/jb.176.1.232-239.1994.Peer-Reviewed Original ResearchConceptsSeryl-tRNA synthetaseYeast seryl-tRNA synthetaseEscherichia coliSerine tRNA geneE. coliConservation of determinantsTRNA genesSchizosaccharomyces pombePrimary transcriptPlasmid promoterAmber suppressionTRNA identityFunctional expressionColiCoexpressionSynthetasePombeGenesPromoterSuppressorTranscriptsOrganismsConservationExpressionEfficient suppression
1993
Yeast seryl‐tRNA synthetase expressed in Escherichia coli recognizes bacterial serine‐specific tRNAs in vivo
WEYGAND‐DURAŠEVIĆ I, Nenad B, Dieter J, Dieter S. Yeast seryl‐tRNA synthetase expressed in Escherichia coli recognizes bacterial serine‐specific tRNAs in vivo. The FEBS Journal 1993, 214: 869-877. PMID: 7686490, DOI: 10.1111/j.1432-1033.1993.tb17990.x.Peer-Reviewed Original ResearchConceptsSeryl-tRNA synthetaseYeast SerRSYeast seryl-tRNA synthetaseEscherichia coliE. coli tRNAVivo complementationProkaryotic hostsTwo-step purificationSer geneHomologous tRNAsNonpermissive temperatureSer mutantE. coli strainsTRNAE. coliColi strainsColiSynthetaseSerRSVivoComplementationMutantsSaccharomycesGenesPromoterThe periplasmic dipeptide permease system transports 5-aminolevulinic acid in Escherichia coli
Verkamp E, Backman V, Björnsson J, Söll D, Eggertsson G. The periplasmic dipeptide permease system transports 5-aminolevulinic acid in Escherichia coli. Journal Of Bacteriology 1993, 175: 1452-1456. PMID: 8444807, PMCID: PMC193232, DOI: 10.1128/jb.175.5.1452-1456.1993.Peer-Reviewed Original ResearchConceptsDpp operonE. coli chromosomeEscherichia coliWild-type growthClasses of mutantsAbsence of ALAGenetic screenDpp mutationsColi chromosomeDpp transportALA biosynthesisFirst geneDipeptide transport systemAnaerobic growthChromosomal insertionOperonRecombinant plasmidTransport systemExogenous ALAALA uptakeE. coliNormal growthMutantsMutationsColi
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
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 chromatography
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 Researchδ-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA
O'Neill G, Chen M, Söll D. δ-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA. FEMS Microbiology Letters 1989, 60: 255-259. DOI: 10.1111/j.1574-6968.1989.tb03482.x.Peer-Reviewed Original ResearchΔ‐Aminolevulinic acid biosynthesisChloroplasts of algaeTRNA-dependent transformationB. subtilisE. coliBacillus subtilisHigher plant speciesEscherichia coliPlant speciesAnaerobic eubacteriaAcid biosynthesisCell-free extractsCell extractsΔ-aminolevulinic acidBiosynthetic activitySubtilisColiGabaculinAbstract Cell-free extractsAnaerobic conditionsAlaEubacteriaArchaebacteriaChloroplastsCyanobacteriadelta-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA.
O'Neill G, Chen M, Söll D. delta-Aminolevulinic acid biosynthesis in Escherichia coli and Bacillus subtilis involves formation of glutamyl-tRNA. FEMS Microbiology Letters 1989, 51: 255-9. PMID: 2511063, DOI: 10.1016/0378-1097(89)90406-0.Peer-Reviewed Original ResearchConceptsDelta-aminolevulinic acid biosynthesisChloroplasts of algaeTRNA-dependent transformationB. subtilisE. coliBacillus subtilisHigher plant speciesEscherichia coliPlant speciesAnaerobic eubacteriaGlutamyl-tRNAAcid biosynthesisCell-free extractsCell extractsBiosynthetic activitySubtilisDelta-aminolevulinic acidColiGabaculinAnaerobic conditionsAlaEubacteriaArchaebacteriaChloroplastsCyanobacteria
1985
supN ochre suppressor gene in Escherichia coli codes for tRNALys
Uemura H, Thorbjarnardóttir S, Gamulin V, Yano J, Andrésson O, Söll D, Eggertsson G. supN ochre suppressor gene in Escherichia coli codes for tRNALys. Journal Of Bacteriology 1985, 163: 1288-1289. PMID: 3897192, PMCID: PMC219277, DOI: 10.1128/jb.163.3.1288-1289.1985.Peer-Reviewed Original ResearchLeucine tRNA family of Escherichia coli: nucleotide sequence of the supP(Am) suppressor gene
Thorbjarnardóttir S, Dingermann T, Rafnar T, Andrésson O, Söll D, Eggertsson G. Leucine tRNA family of Escherichia coli: nucleotide sequence of the supP(Am) suppressor gene. Journal Of Bacteriology 1985, 161: 219-222. PMID: 2981802, PMCID: PMC214859, DOI: 10.1128/jb.161.1.219-222.1985.Peer-Reviewed Original ResearchConceptsSuppressor allelesLeuX geneAmber suppressor allelesMature coding sequenceLeucyl-tRNA synthetaseSingle base changeTRNA familiesCAA anticodonBox sequenceTermination signalDNA sequencesNucleotide sequenceBacteriophage T4Coding sequenceAminoacyl stemSuppressor geneLoop regionTRNABase changesEscherichia coliGenesE. coliSequenceColiAllelesTwo control systems modulate the level of glutaminyl-tRNA synthetase in Escherichia coli
Cheung A, Watson L, Söll D. Two control systems modulate the level of glutaminyl-tRNA synthetase in Escherichia coli. Journal Of Bacteriology 1985, 161: 212-218. PMID: 2578447, PMCID: PMC214858, DOI: 10.1128/jb.161.1.212-218.1985.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseEscherichia coli glutaminyl-tRNA synthetaseBeta-galactosidase structural genePost-transcriptional regulationStructural geneTranscriptional controlRegulatory mutationsTranslational levelGln-10Metabolic regulationEscherichia coliSynthetaseVivo expressionTranscriptionGrowth conditionsRegulationMRNA levelsRegulatory studiesSynthetase levelsMutationsGlnGrowth rateGenesPromoterColi
1982
18 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. coliMutantsMethyltransferaseEnzymeMethyltransferasesRRNANucleotidesIsolationColi
1979
Regulation of the biosynthesis of aminoacyl-transfer ribonucleic acid synthetases and of transfer ribonucleic acid in Escherichia coli. V. Mutants with increased levels of valyl-transfer ribonucleic acid synthetase
Baer M, Low K, Söll D. Regulation of the biosynthesis of aminoacyl-transfer ribonucleic acid synthetases and of transfer ribonucleic acid in Escherichia coli. V. Mutants with increased levels of valyl-transfer ribonucleic acid synthetase. Journal Of Bacteriology 1979, 139: 165-175. PMID: 378953, PMCID: PMC216842, DOI: 10.1128/jb.139.1.165-175.1979.Peer-Reviewed Original ResearchConceptsValyl-tRNA synthetaseAminoacyl-transfer ribonucleic acid synthetasesTransfer ribonucleic acidStructural geneProtein degradationEnzyme overproductionGenetic lociEscherichia coli strainsSpontaneous revertantsEscherichia coliThermolabile enzymeEnzyme synthesisSynthetaseNew enzyme synthesisColi strainsRibonucleic acidRevertantsTurnover rateSynthetasesMutantsBiosynthesisGenesLociColiEnzymeGlutamyl-γ-methyl ester acts as a methionine analogue in Escherichia coli: analogue resistant mutants map at the metJ and metK loci
Kraus J, Soll D, Low K. Glutamyl-γ-methyl ester acts as a methionine analogue in Escherichia coli: analogue resistant mutants map at the metJ and metK loci. Genetics Research 1979, 33: 49-55. PMID: 383574, DOI: 10.1017/s0016672300018152.Peer-Reviewed Original Research
1974
The phenylalanine tRNA from Mycoplasma sp. (Kid): a tRNA lacking hypermodified nucleosides functional in protein synthesis.
Kimball M, Soll D. The phenylalanine tRNA from Mycoplasma sp. (Kid): a tRNA lacking hypermodified nucleosides functional in protein synthesis. Nucleic Acids Research 1974, 1: 1713-20. PMID: 4615304, PMCID: PMC343450.Peer-Reviewed Original ResearchIsolation and Partial Characterization of a Temperature-Sensitive Escherichia coli Mutant with Altered Glutaminyl-Transfer Ribonucleic Acid Synthetase
Körner A, Magee B, Liska B, Low K, Adelberg E, Söll D. Isolation and Partial Characterization of a Temperature-Sensitive Escherichia coli Mutant with Altered Glutaminyl-Transfer Ribonucleic Acid Synthetase. Journal Of Bacteriology 1974, 120: 154-158. PMID: 4153616, PMCID: PMC245744, DOI: 10.1128/jb.120.1.154-158.1974.Peer-Reviewed Original Research