2004
The unusual methanogenic seryl‐tRNA synthetase recognizes tRNASer species from all three kingdoms of life
Bilokapic S, Korencic D, Söll D, Weygand‐Durasevic I. The unusual methanogenic seryl‐tRNA synthetase recognizes tRNASer species from all three kingdoms of life. The FEBS Journal 2004, 271: 694-702. PMID: 14764085, DOI: 10.1111/j.1432-1033.2003.03971.x.Peer-Reviewed Original ResearchMeSH KeywordsAnticodonBase SequenceChromatography, GelDimerizationElectrophoretic Mobility Shift AssayEscherichia coliIsoelectric FocusingMethanococcusMolecular Sequence DataNucleic Acid ConformationProtein BindingRNA, Transfer, Amino AcylRNA, Transfer, SerSerineSerine-tRNA LigaseSubstrate SpecificityTranscription, GeneticYeastsConceptsSeryl-tRNA synthetaseGel mobility shift assaysKingdoms of lifeMobility shift assaysMethanococcus jannaschiiM. maripaludisTRNA recognitionShift assaysTRNARenaturation conditionsGel filtration chromatographyConformation of tRNAComplex formationSpeciesFiltration chromatographySynthetaseDimerizationSerRSsJannaschiiTRNASerIsoacceptorsHomologuesComplementary oligonucleotidesAminoacylationRenaturation
2002
tRNA‐dependent amino acid discrimination by yeast seryl‐tRNA synthetase
Gruic‐Sovulj I, Landeka I, Söll D, Weygand‐Durasevic I. tRNA‐dependent amino acid discrimination by yeast seryl‐tRNA synthetase. The FEBS Journal 2002, 269: 5271-5279. PMID: 12392560, DOI: 10.1046/j.1432-1033.2002.03241.x.Peer-Reviewed Original ResearchConceptsSeryl-tRNA synthetaseYeast seryl-tRNA synthetaseCognate tRNA moleculesAmino acid discriminationAminoacyl-tRNA synthetasesAmino acid substratesSimilar amino acidsAmino acid serineGenetic codeEnzyme active siteTRNA moleculesActive siteYeast SerRSConformational changesAcid substratesAmino acidsSerineSynthetaseStoichiometric analysisDifferent affinitiesEnzymeAccurate translationTRNASerSynthetasesSaccharomyces
1998
C‐terminal truncation of yeast SerRS is toxic for Saccharomyces cerevisiae due to altered mechanism of substrate recognition
Lenhard B, Prætorius-Ibba M, Filipic S, Söll D, Weygand-Durasevic I. C‐terminal truncation of yeast SerRS is toxic for Saccharomyces cerevisiae due to altered mechanism of substrate recognition. FEBS Letters 1998, 439: 235-240. PMID: 9845329, DOI: 10.1016/s0014-5793(98)01376-3.Peer-Reviewed Original ResearchMaize 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
1994
Coexpression 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
Selection of a ‘minimal’ glutaminyl‐tRNA synthetase and the evolution of class I synthetases.
Schwob E, Söll D. Selection of a ‘minimal’ glutaminyl‐tRNA synthetase and the evolution of class I synthetases. The EMBO Journal 1993, 12: 5201-5208. PMID: 7505222, PMCID: PMC413784, DOI: 10.1002/j.1460-2075.1993.tb06215.x.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesBacterial ProteinsBase SequenceBinding SitesBiological EvolutionEscherichia coliModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein Structure, TertiaryRNA, BacterialRNA, Transfer, GlnRNA, Transfer, SerStructure-Activity RelationshipTransfer RNA AminoacylationConceptsGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesEscherichia coli glutaminyl-tRNA synthetaseClass I aminoacyl-tRNA synthetasesNew recognition specificitiesNon-catalytic domainSubstrate recognition propertiesNon-cognate tRNAsRecognition of tRNACommon ancestorSequence motifsAmber suppressorGenetic codeTRNA substratesCatalytic coreGlnRTRNARecognition specificityDistinct domainsEnzymatic activityElaborate relationshipSynthetasesSpecific roleClass ISynthetaseYeast 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 strainsColiSynthetaseSerRSVivoComplementationMutantsSaccharomycesGenesPromoter
1990
Yeast suppressor mutations and transfer RNA processing
Nichols M, Willis I, Söll D. Yeast suppressor mutations and transfer RNA processing. Methods In Enzymology 1990, 181: 377-394. PMID: 2199758, DOI: 10.1016/0076-6879(90)81137-j.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBlotting, NorthernChromosomes, FungalGenes, FungalIndicators and ReagentsMolecular Sequence DataMutationNucleic Acid ConformationNucleic Acid HybridizationRNA Polymerase IIIRNA Processing, Post-TranscriptionalRNA, TransferRNA, Transfer, SerSaccharomyces cerevisiaeSuppression, GeneticTranscription FactorsTranscription, GeneticConceptsTRNA genesMature-sized tRNAsRNA processing reactionsPrimer-directed mutagenesisAminoacyl-tRNA synthetaseTransfer RNA moleculesCognate aminoacyl-tRNA synthetaseRNA processingSuppressor mutationsTRNA locusElongation factorProtein biosynthesisRibosomal interactionsRNA moleculesMutant strainStructural proteinsPink coloniesTranscription efficiencyProcessing reactionsProtein synthesisSuppressor functionTRNALow template concentrationsGenesLoci
1989
Multiple Mutations of the First Gene of a Dimeric tRNA Gene Abolish in Vitro tRNA Gene Transcription
Nichols M, Bell J, Klekamp M, Weil P, Söll D. Multiple Mutations of the First Gene of a Dimeric tRNA Gene Abolish in Vitro tRNA Gene Transcription. Journal Of Biological Chemistry 1989, 264: 17084-17090. PMID: 2676999, DOI: 10.1016/s0021-9258(18)71462-2.Peer-Reviewed Original ResearchMeSH KeywordsCloning, MolecularEndopeptidasesMutationPromoter Regions, GeneticRegulatory Sequences, Nucleic AcidRNA Polymerase IIIRNA, FungalRNA, TransferRNA, Transfer, MetRNA, Transfer, SerSaccharomyces cerevisiaeSchizosaccharomycesTranscription Factor TFIIIBTranscription FactorsTranscription Factors, TFIIITranscription, GeneticConceptsMethionine tRNA geneTRNA genesGene transcriptionInitiator methionine tRNA geneRNA polymerase III systemRNA polymerase III transcriptionMutant tRNA genesTRNA gene transcriptionAdditional protein factorsSerine tRNA genePolymerase III transcriptionRNA polymerase IIIICR sequenceTranscription regulationTRNA locusFirst geneExpression initiatesProtein factorsTranscription studiesPolymerase IIINucleotides 8Gene promoterDetectable transcriptsTranscriptionGenesThe selenocysteine-inserting opal suppressor serine tRNA from E.coli is highly unusual in structure and modification
Schön A, Böck A, Ott G, Sprinzl M, Söll D. The selenocysteine-inserting opal suppressor serine tRNA from E.coli is highly unusual in structure and modification. Nucleic Acids Research 1989, 17: 7159-7165. PMID: 2529478, PMCID: PMC334795, DOI: 10.1093/nar/17.18.7159.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesBase SequenceChromatography, High Pressure LiquidCodonCysteineEscherichia coliGenes, BacterialMolecular Sequence DataNucleic Acid ConformationRNA, Transfer, Amino Acid-SpecificRNA, Transfer, SerSeleniumSelenocysteineStructure-Activity RelationshipSuppression, GeneticSubstrate structural requirements of Schizosaccharomyces pombe RNase P
Drainas D, Zimmerly S, Willis I, Söll D. Substrate structural requirements of Schizosaccharomyces pombe RNase P. FEBS Letters 1989, 251: 84-88. PMID: 2666172, DOI: 10.1016/0014-5793(89)81433-4.Peer-Reviewed Original Research
1988
Genomic organization of tRNA and aminoacyl-tRNA synthetase genes for two amino acids in Saccharomyces cerevisiae
Kolman C, Snyder M, Söll D. Genomic organization of tRNA and aminoacyl-tRNA synthetase genes for two amino acids in Saccharomyces cerevisiae. Genomics 1988, 3: 201-206. PMID: 3066745, DOI: 10.1016/0888-7543(88)90080-8.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthetase genesContour-clamped homogeneous electric field gel electrophoresisHomogeneous electric field gel electrophoresisSynthetase geneGenomic organizationSmall multigene familyDNA gel blotsAmino acidsField gel electrophoresisGel electrophoresisTRNA genesChromosome assignmentMultigene familyGel blotsGene sequencesS. cerevisiaeChromosomal DNATRNAGenesSaccharomycesAspartic acidElectrophoresisGenomeCerevisiaeFamilyDiscrimination 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 ResearchProcessing of histidine transfer RNA precursors. Abnormal cleavage site for RNase P.
Burkard U, Willis I, Söll D. Processing of histidine transfer RNA precursors. Abnormal cleavage site for RNase P. Journal Of Biological Chemistry 1988, 263: 2447-2451. PMID: 3276688, DOI: 10.1016/s0021-9258(18)69227-0.Peer-Reviewed Original Research