2006
Mischarging of M. barkeri tRNAPyl with alanine and serine in vitro
Li D, Polycarpo C, Ambrogelly A, Söll D. Mischarging of M. barkeri tRNAPyl with alanine and serine in vitro. The FASEB Journal 2006, 20: a503-a503. DOI: 10.1096/fasebj.20.4.a503-c.Peer-Reviewed Original ResearchNon-canonical amino acidsSecondary structureCognate tRNA speciesPyrrolysyl-tRNA synthetaseAminoacyl-tRNA synthetaseSimilar secondary structureBovine mitochondriaTRNA speciesAlanine tRNAAnticodon stemAcceptor stemAmino acidsM. barkeriMethanosarcina barkeriSerRSsPyrrolysineMultiple mutationsVariable loopSynthetaseSerineShorter variable loopsSynthetase systemBarkeriAlanineStem
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 stemSynthetasesGlutaminyl-tRNA synthetase.
Freist W, Gauss D, Ibba M, Söll D. Glutaminyl-tRNA synthetase. Biological Chemistry 1997, 378: 1103-17. PMID: 9372179.Peer-Reviewed Original ResearchConceptsE. coli GlnRSGlutaminyl-tRNA synthetaseGlutamyl-tRNA synthetaseMammalian enzymeCommon ancestorPositive eubacteriaCognate tRNAMultienzyme complexTRNA moleculesGlnRArtificial mutantsAcceptor stemAnticodon loopMolecular massAmino acidsCatalytic siteEnzymeSynthetaseEubacteriaArchaebacteriaTRNAMutantsOrganellesAncestorComplexes
1996
Genetic analysis of functional connectivity between substrate recognition domains ofEscherichia coli glutaminyl-tRNA synthetase
Kitabatake M, Inokuchi H, Ibba M, Hong K, Söll D. Genetic analysis of functional connectivity between substrate recognition domains ofEscherichia coli glutaminyl-tRNA synthetase. Molecular Genetics And Genomics 1996, 252: 717-722. PMID: 8917315, DOI: 10.1007/bf02173978.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseWild-type enzymeSubstrate discriminationDouble mutantSubstrate recognition domainThree-dimensional structureAnticodon recognitionSubstrate specificityTRNA bindingGenetic analysisAcceptor stemRecognition domainC171Ternary complexExtensive interactionsMutantsPotential involvementG mutationEnzymeHigh KmSynthetaseMutationsActive siteE222GlnRTransfer RNA-dependent cognate amino acid recognition by an aminoacyl-tRNA synthetase.
Hong K, Ibba M, Weygand-Durasevic I, Rogers M, Thomann H, Söll D. Transfer RNA-dependent cognate amino acid recognition by an aminoacyl-tRNA synthetase. The EMBO Journal 1996, 15: 1983-91. PMID: 8617245, PMCID: PMC450117, DOI: 10.1002/j.1460-2075.1996.tb00549.x.Peer-Reviewed Original ResearchConceptsAmino acid recognitionEscherichia coli glutaminyl-tRNA synthetaseAccuracy of aminoacylationProtein-RNA interactionsRole of tRNAGlutaminyl-tRNA synthetaseAmino acid affinityCharacterization of mutantsAminoacyl-tRNA synthetaseAmino acid activationSpecific interactionsSubstrate recognitionEnzyme active siteGlnRActive siteAcceptor stemTRNAAminoacylationAcid affinityPosition 235TerminusSynthetaseObserved roleGlnTRNAGln
1994
Connecting Anticodon Recognition with the Active Site of Escherichia coli Glutaminyl-tRNA Synthetase
Weygand-Duraševic I, Rogers M, Söll D. Connecting Anticodon Recognition with the Active Site of Escherichia coli Glutaminyl-tRNA Synthetase. Journal Of Molecular Biology 1994, 240: 111-118. PMID: 8027995, DOI: 10.1006/jmbi.1994.1425.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseAnticodon recognitionMutant enzymesEscherichia coli glutaminyl-tRNA synthetaseOpal suppressor tRNASpecificity constantMutant gene productsWild-type enzymeAmino acid loopExtensive conformational changesActive siteNumber of mutationsSuppressor tRNAGene productsGlnRPathways of communicationSaturation mutagenesisTRNAAcceptor stemAcid loopGenetic selectionConformational changesAnticodonPoor substrateAminoacylation
1993
Acceptor end binding domain interactions ensure correct aminoacylation of transfer RNA.
Weygand-Durasević I, Schwob E, Söll D. Acceptor end binding domain interactions ensure correct aminoacylation of transfer RNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 2010-2014. PMID: 7680483, PMCID: PMC46010, DOI: 10.1073/pnas.90.5.2010.Peer-Reviewed Original ResearchConceptsAmber suppressor tRNASuppressor tRNAEscherichia coli glutaminyl-tRNA synthetaseAcceptor stemAccuracy of aminoacylationGlutaminyl-tRNA synthetaseWild-type enzymeNoncognate complexGlnR mutantTRNA specificityArg-130Amber mutationTransfer RNASuch mutantsMutant enzymesCritical residuesDomain contributesDomain interactionsRecognition specificityTRNAGlu-131MutantsNoncognate tRNAsGlnRCorrect aminoacylationSelectivity and specificity in the recognition of tRNA by E coli glutaminyl-tRNA synthetase
Rogers M, Weygand-Durašević I, Schwob E, Sherman J, Rogers K, Adachi T, Inokuchi H, Söll D. Selectivity and specificity in the recognition of tRNA by E coli glutaminyl-tRNA synthetase. Biochimie 1993, 75: 1083-1090. PMID: 8199243, DOI: 10.1016/0300-9084(93)90007-f.Peer-Reviewed Original ResearchConceptsOpal suppressor tRNAGlutaminyl-tRNA synthetaseAcceptor stem recognitionSuppressor tRNAEscherichia coli glutaminyl-tRNA synthetaseGenetic selectionAmber suppressor tRNAExtensive mutational analysisRecognition of tRNARNA contactsTRNA transcriptsRelaxed specificityMutational analysisTRNAGlnRAcceptor stemExtensive proteinIndividual functional groupsMutantsSpecific recognitionAnticodonAminoacylationSynthetaseIdentity elementSynthetases
1991
Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetase
Jahn M, Rogers M, Söll D. Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetase. Nature 1991, 352: 258-260. PMID: 1857423, DOI: 10.1038/352258a0.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseMutant tRNAsE. coli glutaminyl-tRNA synthetaseEfficient amber suppressorsAminoacyl-tRNA synthetasesCorresponding transfer RNASet of nucleotidesMajor recognition elementGlutamine identityAcceptor stem regionTRNA discriminationTransfer RNAAmber suppressorProtein biosynthesisTRNA moleculesUnmodified tRNACorrect attachmentAnticodon regionTRNAAcceptor stemSimilar kinetic parametersEscherichia coliAmino acidsDifferent synthetasesSpecificity constant
1988
Yeast RNase P: catalytic activity and substrate binding are separate functions.
Nichols M, Söll D, Willis I. Yeast RNase P: catalytic activity and substrate binding are separate functions. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 1379-1383. PMID: 3278310, PMCID: PMC279774, DOI: 10.1073/pnas.85.5.1379.Peer-Reviewed Original ResearchConceptsPrecursor tRNAsRNase PSubstrate bindingGel retardationCatalytic functionRibonucleoprotein RNase PDistinct sequence preferencesEnzyme catalytic functionRNase P cleavage siteMature tRNARNase P.Catalytic integrityTRNA precursorsRNA moietyRNA componentSequence preferenceTRNATRNA complexProtein componentsAcceptor stemEnzyme mechanismMaximal cleavageSecond nucleotideCleavage siteEnzymetRNA specificity of a mischarging aminoacyl‐tRNA synthetase: Glutamyl‐tRNA synthetase from barley chloroplasts
Schön A, Söll D. tRNA specificity of a mischarging aminoacyl‐tRNA synthetase: Glutamyl‐tRNA synthetase from barley chloroplasts. FEBS Letters 1988, 228: 241-244. DOI: 10.1016/0014-5793(88)80007-3.Peer-Reviewed Original Research