1998
Major 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
Glutamyl-tRNA sythetase.
Freist W, Gauss D, Söll D, Lapointe J. Glutamyl-tRNA sythetase. Biological Chemistry 1997, 378: 1313-29. PMID: 9426192.Peer-Reviewed Original ResearchConceptsGlutamyl-tRNA synthetaseGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesNegative eubacteriaBacterial glutamyl-tRNA synthetasesATP/PPiHigh molecular mass complexesClass I aminoacyl-tRNA synthetasesCytoplasm of eukaryotesE. coli GlnRSGlutamyl-tRNA synthetasesMolecular mass complexesN-terminal halfC-terminal halfAmino acid residuesDihydrouridine (DHU) armPhylogenetic studiesSpecific amidotransferaseGlutamyl-prolylMass complexesTRNA synthetasesCognate tRNAAcid residuesAcceptor stemSynthetases
1996
Glutamate transfer RNA: a cofactor for heme and chlorophyll biosynthesis.
Madan Kumar A, Söll D. Glutamate transfer RNA: a cofactor for heme and chlorophyll biosynthesis. Indian Journal Of Biochemistry And Biophysics 1996, 33: 30-4. PMID: 8744830.Peer-Reviewed Original Research
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 ResearchDivergence of glutamate and glutamine aminoacylation pathways: Providing the evolutionary rationale for mischarging
Rogers K, Söll D. Divergence of glutamate and glutamine aminoacylation pathways: Providing the evolutionary rationale for mischarging. Journal Of Molecular Evolution 1995, 40: 476-481. PMID: 7783222, DOI: 10.1007/bf00166615.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseGlutamine tRNAEukaryotic organismsProkaryotic organismsGln-tRNAGlnHorizontal gene transfer eventsGene transfer eventsGlutaminyl-tRNA synthetasesGram-negative eubacteriaGlutamyl-tRNA synthetaseAminoacyl-tRNA synthetasesAminoacyl-tRNA synthetaseFamily of enzymesEukaryotic organellesPool of glutamateAminoacyl-tRNATRNADifferent cellular mechanismsEvolutionary rationaleProtein synthesisOrganismsAmino acidsTransfer eventsCellular mechanismsSynthetaseAminoacylation 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
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 synthesisBiosynthesisChloroplastsLight regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis.
Ilag L, Kumar A, Söll D. Light regulation of chlorophyll biosynthesis at the level of 5-aminolevulinate formation in Arabidopsis. The Plant Cell 1994, 6: 265-275. PMID: 7908550, PMCID: PMC160432, DOI: 10.1105/tpc.6.2.265.Peer-Reviewed Original ResearchMeSH KeywordsAldehyde OxidoreductasesAmino Acid SequenceAminolevulinic AcidArabidopsisChlorophyllChloroplastsEscherichia coliGene Expression RegulationGenes, PlantGlutamatesGlutamic AcidIntramolecular TransferasesIsomerasesLightMolecular Sequence DataPromoter Regions, GeneticRNA, Transfer, GluSequence Homology, Amino AcidSequence Homology, Nucleic AcidTranscription, GeneticConceptsC5 pathwayAmino acid sequenceHemA proteinChlorophyll biosynthesisGlu-tRNAALA formationAcid sequenceRNA gel blot analysisDeduced amino acid sequenceGlu-tRNA reductaseChloroplasts of plantsGel blot analysisArabidopsis genesFunctional complementationShort intronsCorresponding genesTranscriptional controlFlower tissuesLight regulationExtensive homologyFirst enzymeUniversal precursorReductase geneChlorophyll formationSecond enzyme
1993
Discrimination among tRNAs intermediate in glutamate and glutamine acceptor identity.
Rogers K, Söll D. Discrimination among tRNAs intermediate in glutamate and glutamine acceptor identity. Biochemistry 1993, 32: 14210-9. PMID: 7505112, DOI: 10.1021/bi00214a021.Peer-Reviewed Original ResearchAmino Acyl-tRNA SynthetasesAnticodonBase SequenceBiological EvolutionEscherichia coliGlutamate-tRNA LigaseHydrogen BondingKineticsMolecular Sequence DataNucleic Acid ConformationRNA, BacterialRNA, Transfer, GlnRNA, Transfer, GluStructure-Activity RelationshipSubstrate SpecificityTransfer RNA AminoacylationA 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase.
Sylvers L, Rogers K, Shimizu M, Ohtsuka E, Söll D. A 2-thiouridine derivative in tRNAGlu is a positive determinant for aminoacylation by Escherichia coli glutamyl-tRNA synthetase. Biochemistry 1993, 32: 3836-41. PMID: 8385989, DOI: 10.1021/bi00066a002.Peer-Reviewed Original ResearchThe recognition of E. coli glutamine tRNA by glutaminyl-tRNA synthetase.
Rogers M, Weygand-Durasević I, Schwob E, Sherman J, Rogers K, Thomann H, Sylvers L, Ohtsuka E, Inokuchi H, Söll D. The recognition of E. coli glutamine tRNA by glutaminyl-tRNA synthetase. Nucleic Acids Symposium Series 1993, 211-3. PMID: 7504247.Peer-Reviewed Original Research
1992
Synthetase competition and tRNA context determine the in vivo identity of tRNA discriminator mutants
Sherman J, Rogers K, Rogers M, Söll D. Synthetase competition and tRNA context determine the in vivo identity of tRNA discriminator mutants. Journal Of Molecular Biology 1992, 228: 1055-1062. PMID: 1474577, DOI: 10.1016/0022-2836(92)90314-a.Peer-Reviewed Original ResearchConceptsAmber suppressorTyrosine tRNAN-terminal protein sequencingGlutamyl-tRNA synthetaseE. coli dihydrofolate reductaseAminoacyl-tRNA synthetasesEffects of mutationsEfficiency of aminoacylationColi dihydrofolate reductaseSite of aminoacylationTyrosine specificityTRNAs exhibitGlutamine tRNAMutagenic analysisProtein sequencingGlutamate tRNAImportant identity elementVivo identityTRNANucleotide substitutionsTRNA identityDiscriminator baseDihydrofolate reductaseMultiple mutationsSynthetasesChloroplast tRNAAsp: nucleotide sequence and variation of in vivo levels during plastid maturation
Schön A, Gough S, Söll D. Chloroplast tRNAAsp: nucleotide sequence and variation of in vivo levels during plastid maturation. Plant Molecular Biology 1992, 20: 601-607. PMID: 1450377, DOI: 10.1007/bf00046445.Peer-Reviewed Original ResearchCompetition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation
Sherman J, Rogers M, Söll D. Competition of aminoacyl-tRNA synthetases for tRNA ensures the accuracy of aminoacylation. Nucleic Acids Research 1992, 20: 2847-2852. PMID: 1377381, PMCID: PMC336931, DOI: 10.1093/nar/20.11.2847.Peer-Reviewed Original ResearchConceptsAccuracy of aminoacylationAminoacyl-tRNA synthetasesTyrosyl-tRNA synthetaseE. coli tyrosyl-tRNA synthetaseEscherichia coli tyrosyl-tRNA synthetaseGlutaminyl-tRNA synthetaseLevel of aminoacylationProtein biosynthesisTRNASynthetasesAminoacylationCompetition assaysDiscriminator baseDifferent synthetasesConcurrent overexpressionCorrect aminoacylationSynthetaseFirst baseRelative affinityVivoMisacylationAssaysAnticodonBiosynthesisCompetition
1990
Expression of the Synechocystis sp. strain PCC 6803 tRNA(Glu) gene provides tRNA for protein and chlorophyll biosynthesis
O'Neill G, Söll D. Expression of the Synechocystis sp. strain PCC 6803 tRNA(Glu) gene provides tRNA for protein and chlorophyll biosynthesis. Journal Of Bacteriology 1990, 172: 6363-6371. PMID: 2121711, PMCID: PMC526821, DOI: 10.1128/jb.172.11.6363-6371.1990.Peer-Reviewed Original ResearchConceptsSynechocystis 6803Synechocystis spFirst anticodon baseStrain PCC 6803Cyanobacterium Synechocystis spTotal tRNA populationAmount of chlorophyllNorthern blot analysisChlorophyll biosynthesisALA biosynthesisPrecursor tRNAsPCC 6803TRNA speciesProtein biosynthesisTRNA populationCellular RNAAminoacylation assaysChlorophyll levelsBiosynthesisAddition of inhibitorsBlot analysisTranslation systemDelta-aminolevulinic acidTRNAChlorophyllSequence of tRNAGlu and its genes from the chloroplast genome of Chlamydomonas reinhardtii
O'Neill G, Schön A, Chow H, Chen M, Kim Y, Söll D. Sequence of tRNAGlu and its genes from the chloroplast genome of Chlamydomonas reinhardtii. Nucleic Acids Research 1990, 18: 5893-5893. PMID: 2216788, PMCID: PMC332342, DOI: 10.1093/nar/18.19.5893.Peer-Reviewed Original ResearchTransfer RNA and the formation of the heme and chlorophyll precursor, 5-aminolevulinic acid.
O'Neill G, Söll D. Transfer RNA and the formation of the heme and chlorophyll precursor, 5-aminolevulinic acid. BioFactors 1990, 2: 227-35. PMID: 2282139.Peer-Reviewed Original ResearchConceptsGlu-tRNA reductaseSequence-specific recognitionDual-function moleculeNADPH-dependent enzymeThree-step pathwayTransfer RNASpecific cofactorsChlorophyll precursorsLow molecular weight metabolitesNovel roleAmino acidsReduction of glutamatePeptide bond synthesisTRNAWeight metabolitesHemeMetabolic conversionBond synthesisBiosynthesisRNAOrganismsAcidCofactorProteinGlutamate
1989
delta-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
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 ResearchFormation of the chlorophyll precursor delta-aminolevulinic acid in cyanobacteria requires aminoacylation of a tRNAGlu species
O'Neill G, Peterson D, Schön A, Chen M, Söll D. Formation of the chlorophyll precursor delta-aminolevulinic acid in cyanobacteria requires aminoacylation of a tRNAGlu species. Journal Of Bacteriology 1988, 170: 3810-3816. PMID: 2900830, PMCID: PMC211375, DOI: 10.1128/jb.170.9.3810-3816.1988.Peer-Reviewed Original ResearchConceptsPrecursor delta-aminolevulinic acidHigher plantsUnicellular cyanobacterium Synechocystis spGlutamate-1-semialdehyde aminotransferaseCell extractsCyanobacterium Synechocystis spDelta-aminolevulinic acidSouthern blot analysisIdentical primary sequencesSynechocystis spNucleotide modificationsConversion of glutamateGene copiesALA synthesisPrimary sequenceSequence specificityTerminal enzymePolyacrylamide gel electrophoresisChloroplastsEuglena gracilisEscherichia coliSpeciesBlot analysisTRNAGel electrophoresis