2003
Non-canonical Eukaryotic Glutaminyl- and Glutamyl-tRNA Synthetases Form Mitochondrial Aminoacyl-tRNA in Trypanosoma brucei *
Rinehart J, Horn EK, Wei D, Söll D, Schneider A. Non-canonical Eukaryotic Glutaminyl- and Glutamyl-tRNA Synthetases Form Mitochondrial Aminoacyl-tRNA in Trypanosoma brucei *. Journal Of Biological Chemistry 2003, 279: 1161-1166. PMID: 14563839, DOI: 10.1074/jbc.m310100200.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseGlutamyl-tRNA synthetaseT. bruceiGln-tRNATrypanosoma bruceiInsect stage T. bruceiT. brucei enzymeRespective gene productsAminoacyl-tRNA synthetasesGlutamyl-tRNA synthetase activitySynthetase activityTransamidation pathwayLeishmania mitochondriaBrucei enzymeMitochondrial tRNAsGlu-tRNAProtein biosynthesisAminoacylation experimentsGene productsRNA interferenceTRNABruceiMitochondriaTotal tRNAGlutaminyl
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 analysisAmidotransferaseSynthetaseGenesConserved amino acids near the carboxy terminus of bacterial tyrosyl‐tRNA synthetase are involved in tRNA and Tyr‐AMP binding
Salazar J, Zuñiga R, Lefimil C, Söll D, Orellana O. Conserved amino acids near the carboxy terminus of bacterial tyrosyl‐tRNA synthetase are involved in tRNA and Tyr‐AMP binding. FEBS Letters 2001, 491: 257-260. PMID: 11240138, DOI: 10.1016/s0014-5793(01)02214-1.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine MonophosphateBacterial ProteinsCloning, MolecularConserved SequenceDimerizationEscherichia coliGammaproteobacteriaGene ExpressionGenetic Complementation TestGeobacillus stearothermophilusMutagenesis, Site-DirectedRNA, TransferSequence Homology, Amino AcidStructure-Activity RelationshipTyrosineTyrosine-tRNA LigaseConceptsBacterial tyrosyl-tRNA synthetasesBacterial tyrosyl tRNA synthetaseConserved amino acidsAmino acidsAmino acid identityAmino-terminal regionActive site domainCarboxy-terminal segmentTyrosyl-tRNA synthetasesTyrosyl-tRNA synthetaseAcid identityLargest subfamilyCarboxy terminusSite domainTRNA bindingEnzyme functionTyr-AMPTRNATyrRSResiduesEquivalent roleBindingH306S356K395
2000
Domain-specific recruitment of amide amino acids for protein synthesis
Tumbula D, Becker H, Chang W, Söll D. Domain-specific recruitment of amide amino acids for protein synthesis. Nature 2000, 407: 106-110. PMID: 10993083, DOI: 10.1038/35024120.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseAsparaginyl-tRNA synthetaseProtein synthesisAmino acidsAminoacyl-transfer RNAAmino acid metabolismGlu-tRNAGlnAsn-tRNAProtein biosynthesisGln-tRNAArchaeaTRNASynthetaseAmidotransferaseBacteriaAmidotransferasesDirect evidenceDifferent mechanismsBiosynthesisCentral importanceCrucial stepRNAOrganismsDomainCytoplasmThe 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
1999
Cysteinyl‐tRNA formation: the last puzzle of aminoacyl‐tRNA synthesis
Li T, Graham D, Stathopoulos C, Haney P, Kim H, Vothknecht U, Kitabatake M, Hong K, Eggertsson G, Curnow A, Lin W, Celic I, Whitman W, Söll D. Cysteinyl‐tRNA formation: the last puzzle of aminoacyl‐tRNA synthesis. FEBS Letters 1999, 462: 302-306. PMID: 10622715, DOI: 10.1016/s0014-5793(99)01550-1.Peer-Reviewed Original ResearchConceptsLateral gene transferAminoacyl-tRNA synthesisCysteinyl-tRNA synthetaseEscherichia coli cysteinyl-tRNA synthetaseMolecular phylogenyPyrococcus sppMethanococcus jannaschiiMethanococcus maripaludisM. maripaludisMethanogenic archaeaMethanosarcina sppGene transferCysRSMethanosarcina barkeriGenesSpecific relativeLast puzzleSppOrthologsArchaeaPhylogenyJannaschiiMutantsLineagesOrganismsSubstrate recognition by class I lysyl-tRNA synthetases: A molecular basis for gene displacement
Ibba M, Losey H, Kawarabayasi Y, Kikuchi H, Bunjun S, Söll D. Substrate recognition by class I lysyl-tRNA synthetases: A molecular basis for gene displacement. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 418-423. PMID: 9892648, PMCID: PMC15151, DOI: 10.1073/pnas.96.2.418.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesBase SequenceBorrelia burgdorferi GroupCloning, MolecularDiphosphatesEscherichia coliEvolution, MolecularGenes, ArchaealGenes, BacterialGenetic Complementation TestKineticsLysine-tRNA LigaseMethanococcusMolecular Sequence DataNucleic Acid ConformationPhylogenyRNA, Transfer, Amino AcylSequence Analysis, DNASubstrate SpecificityTranscription, GeneticConceptsClass II LysRSAminoacyl-tRNA synthetasesLysyl-tRNA synthetasesSubstrate recognitionMolecular basisBacterial class IClass II enzymesSequence-specific recognitionGene displacementTranslational apparatusTRNA recognitionEscherichia coli strainsLysRSLysRSsSame nucleotideSynthetasesDiscriminator baseUnrelated typesLysine activationCertain bacteriaII enzymesColi strainsTRNALysClass IEnzyme
1998
Sequence Divergence of Seryl-tRNA Synthetases in Archaea
Kim H, Vothknecht U, Hedderich R, Celic I, Söll D. Sequence Divergence of Seryl-tRNA Synthetases in Archaea. Journal Of Bacteriology 1998, 180: 6446-6449. PMID: 9851985, PMCID: PMC107743, DOI: 10.1128/jb.180.24.6446-6449.1998.Peer-Reviewed Original ResearchConceptsOpen reading frameM. thermoautotrophicumRelevant open reading frameSeryl-tRNA synthetasesCys-tRNACysCanonical cysteinyl-tRNA synthetaseGel shift experimentsCysteinyl-tRNA synthetaseN-terminal peptide sequenceEscherichia coli tRNASequence divergenceDirect aminoacylationM. jannaschiiMethanococcus jannaschiiGenomic sequencesReading frameSer geneHomologous tRNAsGenomic dataMethanogenic archaeaMethanobacterium thermoautotrophicumShift experimentsEnzymatic propertiesArchaeaSerineGlutamyl-tRNAGln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis
Curnow A, Tumbula D, Pelaschier J, Min B, Söll D. Glutamyl-tRNAGln amidotransferase in Deinococcus radiodurans may be confined to asparagine biosynthesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 12838-12843. PMID: 9789001, PMCID: PMC23620, DOI: 10.1073/pnas.95.22.12838.Peer-Reviewed Original ResearchConceptsDeinococcus radioduransD. radiodurans genomeRadiation-resistant bacterium Deinococcus radioduransBiosynthesis of asparagineGlutaminyl-tRNA synthetaseGlutamyl-tRNA synthetaseBacterium Deinococcus radioduransPresence of AsnRSAsparaginyl-tRNA synthetaseAspartyl-tRNA synthetaseAsn-tRNAAsparagine biosynthesisAsparaginyl-tRNAGenomic sequencesGln-tRNAAsparagine synthetaseBiochemical experimentsTransamidation activityGlutaminyl-tRNAProtein synthesisSingle enzymeSynthetaseRadioduransBiosynthesisGenesMaize 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 substrateSynthetaseColiSynthetasesTRNAVivoCDNAMaizeEnzymeMajor Identity Element of Glutamine tRNAs from Bacillus subtilis and Escherichia coli in the Reaction with B. subtilis Glutamyl-tRNA Synthetase
Kim S, Söll D. Major Identity Element of Glutamine tRNAs from Bacillus subtilis and Escherichia coli in the Reaction with B. subtilis Glutamyl-tRNA Synthetase. Molecules And Cells 1998, 8: 459-465. PMID: 9749534, DOI: 10.1016/s1016-8478(23)13451-0.Peer-Reviewed Original Research
1997
A Euryarchaeal Lysyl-tRNA Synthetase: Resemblance to Class I Synthetases
Ibba M, Morgan S, Curnow A, Pridmore D, Vothknecht U, Gardner W, Lin W, Woese C, Söll D. A Euryarchaeal Lysyl-tRNA Synthetase: Resemblance to Class I Synthetases. Science 1997, 278: 1119-1122. PMID: 9353192, DOI: 10.1126/science.278.5340.1119.Peer-Reviewed Original ResearchConceptsClass I aminoacyl-tRNA synthetaseCrenarchaeote Sulfolobus solfataricusDinucleotide-binding domainAminoacyl-tRNA synthetasesAmino acid motifsAmino acid sequenceAminoacyl-tRNA synthetaseLysyl-tRNA synthetaseClass II synthetasesEuryarchaeal genomesUnassigned functionMethanococcus jannaschiiMethanococcus maripaludisLysRS proteinsReading frameSulfolobus solfataricusAcid motifAcid sequenceSuch organismsMethanobacterium thermoautotrophicumLysRSProteinSynthetasesSynthetaseRNA synthetase
1996
Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme.
Ibba M, Hong K, Sherman J, Sever S, Söll D. Interactions between tRNA identity nucleotides and their recognition sites in glutaminyl-tRNA synthetase determine the cognate amino acid affinity of the enzyme. Proceedings Of The National Academy Of Sciences Of The United States Of America 1996, 93: 6953-6958. PMID: 8692925, PMCID: PMC38915, DOI: 10.1073/pnas.93.14.6953.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesAnimalsBase SequenceBinding SitesCalorimetryCloning, MolecularConsensus SequenceEscherichia coliHumansKineticsModels, StructuralMolecular Sequence DataNucleic Acid ConformationProtein FoldingRecombinant ProteinsRNA, Transfer, GlnSequence Homology, Nucleic AcidConceptsGlutaminyl-tRNA synthetaseAmino acid affinityAmino acid recognitionEscherichia coli glutaminyl-tRNA synthetaseBase pairsIdentity nucleotidesProtein-RNA interactionsDiscriminator baseE. coli tryptophanyl-tRNA synthetaseAminoacyl-tRNA synthetasesSequence-specific interactionsAcid affinityRecognition sitesAbility of tRNATryptophanyl-tRNA synthetaseTRNA specificityNoncognate substratesTranslational fidelityTRNA recognitionBiochemical functionsRNA recognitionCognate tRNATRNAMajor binding siteNoncognate tRNAsA mutation in protein phosphatase 2A regulatory subunit A affects auxin transport in Arabidopsis.
Garbers C, DeLong A, Deruére J, Bernasconi P, Söll D. A mutation in protein phosphatase 2A regulatory subunit A affects auxin transport in Arabidopsis. The EMBO Journal 1996, 15: 2115-2124. PMID: 8641277, PMCID: PMC450134, DOI: 10.1002/j.1460-2075.1996.tb00565.x.Peer-Reviewed Original ResearchConceptsProtein phosphatase 2AAuxin transportNaphthylphthalamic acidPhosphatase 2AProtein phosphatase 2A regulatory subunitT-DNA insertionRoot hair developmentT-DNA insertsTemperature-sensitive phenotypeRcn1 mutationROOTS CURLPhytohormone auxinArabidopsis thalianaMutant phenotypeAuxin effluxRCN1 geneRegulatory subunitHypocotyl elongationRoot branchingCell elongationShoot apexMolecular mechanismsHair developmentArabidopsisGrowth curvatureEscherichia coli Tryptophanyl-tRNA Synthetase Mutants Selected for Tryptophan Auxotrophy Implicate the Dimer Interface in Optimizing Amino Acid Binding †
Sever S, Rogers K, Rogers M, Carter C, Söll D. Escherichia coli Tryptophanyl-tRNA Synthetase Mutants Selected for Tryptophan Auxotrophy Implicate the Dimer Interface in Optimizing Amino Acid Binding †. Biochemistry 1996, 35: 32-40. PMID: 8555191, DOI: 10.1021/bi952103d.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBacillus subtilisBase SequenceBinding SitesCloning, MolecularDNA PrimersEscherichia coliGenes, BacterialGeobacillus stearothermophilusHaemophilus influenzaeKineticsMacromolecular SubstancesModels, MolecularMolecular Sequence DataPolymerase Chain ReactionProtein FoldingProtein Structure, SecondaryRecombinant ProteinsRestriction MappingSequence Homology, Amino AcidTryptophanTryptophan-tRNA LigaseConceptsTryptophanyl-tRNA synthetaseDimer interfaceClass I aminoacyl-tRNA synthetasesAminoacyl-tRNA synthetasesAmino acid bindingAmino acid activationActive siteSteady-state kinetic analysisSynthetase mutantsRossmann foldApparent KmKMSKS loopTrp lociProtein structureTrpR proteinTryptophan auxotrophDimeric enzymeAuxotrophic strainsBacillus stearothermophilusAcid bindingEscherichia coliOptimal catalysisAminoacyl adenylatesMutantsMutations
1994
A point mutation in Euglena gracilis chloroplast tRNA(Glu) uncouples protein and chlorophyll biosynthesis.
Stange-Thomann N, Thomann H, Lloyd A, Lyman H, Söll D. A point mutation in Euglena gracilis chloroplast tRNA(Glu) uncouples protein and chlorophyll biosynthesis. Proceedings Of The National Academy Of Sciences Of The United States Of America 1994, 91: 7947-7951. PMID: 8058739, PMCID: PMC44521, DOI: 10.1073/pnas.91.17.7947.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde OxidoreductasesAnimalsBase SequenceBlotting, NorthernChlorophyllChloroplastsCloning, MolecularDNADNA PrimersEuglena gracilisIntramolecular TransferasesIsomerasesMolecular Sequence DataNucleic Acid ConformationPoint MutationPolymerase Chain ReactionProtein BiosynthesisRNA, Transfer, GluConceptsEuglena gracilis chloroplastsChlorophyll biosynthesisGlu-tRNA reductaseChlorophyll-deficient mutantsPoint mutationsChloroplast protein synthesisSequence-specific mannerDual-function moleculeC5 pathwayNADPH-dependent reductionSpecific cofactorsGluTRFirst enzymeGene productsUniversal precursorImportant identity elementAminomutase activitySequence analysisE. gracilisSecond enzymeTetrapyrrole pigmentsT-loopProtein synthesisBiosynthesisChloroplasts
1993
Two members of the ERabp gene family are expressed differentially in reproductive organs but to similar levels in the coleoptile of maize
Hesse T, Garbers C, Brzobohaty B, Kreimer G, Söll D, Melkonian M, Schell J, Palme K. Two members of the ERabp gene family are expressed differentially in reproductive organs but to similar levels in the coleoptile of maize. Plant Molecular Biology 1993, 23: 57-66. PMID: 8219056, DOI: 10.1007/bf00021419.Peer-Reviewed Original ResearchConceptsC-terminal KDEL motifExpression patternsN-terminal hydrophobic leader sequenceColeoptiles of maizePrimary amino acid sequenceFemale flower partsHydrophobic leader sequenceAmino acid sequencePotential glycosylation sitesGene familyFlower organsKDEL motifProtein familyCDNA clonesLeader sequenceMaize seedlingsAcid sequenceGlycosylation sitesPrimary leavesFlower partsGenesLaser scanning microscopyRetention of proteinsReproductive organsNew member
1992
Arabidopsis alternative oxidase sustains Escherichia coli respiration.
Kumar A, Söll D. Arabidopsis alternative oxidase sustains Escherichia coli respiration. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 10842-10846. PMID: 1438286, PMCID: PMC50438, DOI: 10.1073/pnas.89.22.10842.Peer-Reviewed Original ResearchConceptsAlternative oxidaseArabidopsis thaliana cDNA libraryGlutamyl-tRNA reductaseCyanide-insensitive respiratory pathwayAlternative oxidase activityAmino acid sequenceArabidopsis proteinsHemA geneMolecular biological investigationsCDNA libraryFirst enzymeAcid sequenceSauromatum guttatumEscherichia coli strainsSingle polypeptideRespiratory pathwayAerobic respirationRedox enzymesE. coliColi strainsPorphyrin biosynthesisGenesEnzymeProteinBiological investigationsSwitching tRNA(Gln) identity from glutamine to tryptophan.
Rogers M, Adachi T, Inokuchi H, Söll D. Switching tRNA(Gln) identity from glutamine to tryptophan. Proceedings Of The National Academy Of Sciences Of The United States Of America 1992, 89: 3463-3467. PMID: 1565639, PMCID: PMC48888, DOI: 10.1073/pnas.89.8.3463.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesAnticodonBase SequenceBeta-GalactosidaseCloning, MolecularEscherichia coliGenes, BacterialGenes, SuppressorGenes, SyntheticGlutamineMolecular Sequence DataMutagenesis, Site-DirectedNucleic Acid ConformationRNA, Transfer, GlnSuppression, GeneticTetrahydrofolate DehydrogenaseTryptophanConceptsOpal suppressorEscherichia coli glutaminyl-tRNA synthetaseAccuracy of aminoacylationGlutaminyl-tRNA synthetaseN-terminal sequence analysisEfficient suppressorYeast mitochondriaRespective tRNAsUCA anticodonAmber suppressorFol geneUGA codonUGA mutationsSequence analysisAlanine insertionAnticodonGenetic selectionBase pairsBase substitutionsSuppressorTRNATrpRSDihydrofolate reductasePosition 35Mutations
1991
The Escherichia coli hemL gene encodes glutamate 1-semialdehyde aminotransferase
Ilag L, Jahn D, Eggertsson G, Söll D. The Escherichia coli hemL gene encodes glutamate 1-semialdehyde aminotransferase. Journal Of Bacteriology 1991, 173: 3408-3413. PMID: 2045363, PMCID: PMC207952, DOI: 10.1128/jb.173.11.3408-3413.1991.Peer-Reviewed Original ResearchMeSH KeywordsAminolevulinic AcidCentrifugation, Density GradientChromatography, High Pressure LiquidCloning, MolecularDose-Response Relationship, DrugElectrophoresis, Polyacrylamide GelEscherichia coliIntramolecular TransferasesIsomerasesMolecular WeightPyridoxal PhosphatePyridoxamineTransformation, GeneticConceptsGlu-tRNA reductaseTRNA-dependent transformationApparent native molecular massMolecular massGlutamyl-tRNA synthetaseNative molecular massAminoglycoside antibiotic kanamycinHemL geneWild-type DNAAuxotrophic phenotypeC5 pathwaySodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisMap positionGSA aminotransferasePhysical mappingSulfate-polyacrylamide gel electrophoresisRate zonal sedimentationGene productsThird enzymeGlycerol gradientsApparent homogeneityAntibiotic kanamycinEscherichia coliPure protein