2018
Transfer RNA function and evolution
O’Donoghue P, Ling J, Söll D. Transfer RNA function and evolution. RNA Biology 2018, 15: 423-426. PMID: 30099966, PMCID: PMC6103721, DOI: 10.1080/15476286.2018.1478942.Peer-Reviewed Original Research
2000
AMINOACYL-tRNA SYNTHESIS
Ibba M, Söll D. AMINOACYL-tRNA SYNTHESIS. Annual Review Of Biochemistry 2000, 69: 617-650. PMID: 10966471, DOI: 10.1146/annurev.biochem.69.1.617.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsBacteriaBacterial InfectionsBiological EvolutionEnzyme InhibitorsHumansModels, MolecularRNA, Transfer, Amino AcylConceptsAminoacyl-tRNA synthesisAmino acidsAminoacyl-tRNA synthetaseEvolutionary facetsWhole-genome sequencingCorresponding tRNAsGenetic codeGenome sequencingAminoacyl-tRNACorresponding anticodonTRNACurrent knowledgeStructural dataRecent studiesAnticodonDetailed pictureAcidSequencingSynthetaseEditingProofreadingSynthesisTranslationDirect attachment
1995
Divergence 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
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 ISynthetaseDiscrimination 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 Aminoacylation
1989
Structure of E. coli Glutaminyl-tRNA Synthetase Complexed with tRNAGln and ATP at 2.8 Å Resolution
Rould M, Perona J, Söll D, Steitz T. Structure of E. coli Glutaminyl-tRNA Synthetase Complexed with tRNAGln and ATP at 2.8 Å Resolution. Science 1989, 246: 1135-1142. PMID: 2479982, DOI: 10.1126/science.2479982.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino Acyl-tRNA SynthetasesAnticodonBase CompositionBase SequenceBinding SitesBiological EvolutionChemical PhenomenaChemistry, PhysicalCrystallizationEscherichia coliMolecular Sequence DataMolecular StructureNucleic Acid ConformationRNA, BacterialRNA, FungalRNA, Transfer, Amino Acid-SpecificRNA, Transfer, GlnX-Ray Diffraction
1986
Functional complementation between mutations in a yeast suppressor tRNA gene reveals potential for evolution of tRNA sequences.
Willis I, Nichols M, Chisholm V, Söll D, Heyer W, Szankasi P, Amstutz H, Munz P, Kohli J. Functional complementation between mutations in a yeast suppressor tRNA gene reveals potential for evolution of tRNA sequences. Proceedings Of The National Academy Of Sciences Of The United States Of America 1986, 83: 7860-7864. PMID: 3532123, PMCID: PMC386822, DOI: 10.1073/pnas.83.20.7860.Peer-Reviewed Original ResearchConceptsMutant tRNA precursorS. pombe genesSuppressor tRNA geneNucleotide sequence evolutionRNA processing levelRNase P cleavagePombe geneTRNA genesFunctional complementationComplementation eventsS. pombeCycle of inactivationTRNA sequencesTRNA precursorsSequence evolutionSaccharomyces cerevisiaeS. cerevisiaePombe strainSchizosaccharomyces pombe strainStructural domainsDifferential expressionSuppressor functionP cleavageGenesSuppressor
1985
Nucleotide sequences of two serine tRNAs with a GGA anticodon: the structure-function relationships in the serine family of E. coli tRNAs
Grosjean H, Nicoghosian K, Haumont E, Söll D, Cedergren R. Nucleotide sequences of two serine tRNAs with a GGA anticodon: the structure-function relationships in the serine family of E. coli tRNAs. Nucleic Acids Research 1985, 13: 5697-5706. PMID: 3898020, PMCID: PMC321899, DOI: 10.1093/nar/13.15.5697.Peer-Reviewed Original ResearchConceptsSerine tRNANucleotide sequenceRecent common ancestorE. coli tRNACodon-anticodon interactionStructure-function relationshipsEubacterial originUCU codonsEvolutionary analysisCommon ancestorD-loopTRNAAnticodon stemSerine familyAnticodonGenesE. coliMinor speciesCodonMajor speciesSpeciesSequenceTRNASerAncestorSerineConservation and variability of wheat α/β-gliadin genes
Sumner-Smith M, Rafalski J, Sugiyama T, Stoll M, Sōll D. Conservation and variability of wheat α/β-gliadin genes. Nucleic Acids Research 1985, 13: 3905-3916. PMID: 3839304, PMCID: PMC341285, DOI: 10.1093/nar/13.11.3905.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceBase SequenceBiological EvolutionCloning, MolecularDNAGenesGenetic VariationGliadinMutationPlant ProteinsPlantsRNA, MessengerTriticumConceptsTypical eukaryotic promoterStorage protein genesEvolutionary relatednessGenomic clonesGliadin genesEukaryotic promotersGliadin familyProtein genePolyadenylation signalPolyglutamine stretchGene multiplicationClose homologyGlutamine codonGenesCertain mutationsCodonUnusual structureP-boxesIntronsHomologyPromoterPlantsProlineClonesRelatedness
1976
Studies of the complex between transfer RNAs with complementary anticodons I. Origins of enhanced affinity between complementary triplets
Grosjean H, Söll D, Crothers D. Studies of the complex between transfer RNAs with complementary anticodons I. Origins of enhanced affinity between complementary triplets. Journal Of Molecular Biology 1976, 103: 499-519. PMID: 781277, DOI: 10.1016/0022-2836(76)90214-x.Peer-Reviewed Original Research