2022
Unconventional genetic code systems in archaea
Meng K, Chung CZ, Söll D, Krahn N. Unconventional genetic code systems in archaea. Frontiers In Microbiology 2022, 13: 1007832. PMID: 36160229, PMCID: PMC9499178, DOI: 10.3389/fmicb.2022.1007832.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsGenetic code systemAmino acidsTRNA-dependent pathwayCanonical amino acidsRare amino acidArchaeal lineagesArchaeal speciesSingle lineageArchaeaMolecular mechanismsThird domainExtreme environmentsRecent discoveryLineagesBiochemical elementsHarsh conditionsEukaryotesPyrrolysineSelenocysteineOrganismsSpeciesBacteriaPathwayAcidDiscovery
2020
Front Cover: Hijacking Translation Initiation for Synthetic Biology (ChemBioChem 10/2020)
Tharp J, Krahn N, Varshney U, Söll D. Front Cover: Hijacking Translation Initiation for Synthetic Biology (ChemBioChem 10/2020). ChemBioChem 2020, 21: 1383-1383. DOI: 10.1002/cbic.202000239.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus Statements
2019
Translation of Diverse Aramid- and 1,3-Dicarbonyl-peptides by Wild Type Ribosomes in Vitro
Ad O, Hoffman KS, Cairns AG, Featherston AL, Miller SJ, Söll D, Schepartz A. Translation of Diverse Aramid- and 1,3-Dicarbonyl-peptides by Wild Type Ribosomes in Vitro. ACS Central Science 2019, 5: 1289-1294. PMID: 31403077, PMCID: PMC6661870, DOI: 10.1021/acscentsci.9b00460.Peer-Reviewed Original Research
2014
Exploring the Substrate Range of Wild‐Type Aminoacyl‐tRNA Synthetases
Fan C, Ho JM, Chirathivat N, Söll D, Wang Y. Exploring the Substrate Range of Wild‐Type Aminoacyl‐tRNA Synthetases. ChemBioChem 2014, 15: 1805-1809. PMID: 24890918, PMCID: PMC4133344, DOI: 10.1002/cbic.201402083.Peer-Reviewed Original ResearchConceptsAminoacyl-tRNA synthetasesSubstrate rangeDifferent amino acid sitesAmino acidsE. coli tryptophanyl-tRNA synthetaseE. coli aminoacyl-tRNA synthetasesAmino acid sitesCanonical amino acidsNonstandard amino acidsTyrosyl-tRNA synthetaseTryptophanyl-tRNA synthetaseAnticodon sequenceTRNA synthetasesSynthetasesSynthetaseSequenceAnticodonNSAAsTrpRSProteinAminoacylAcid
2008
Pyrrolysyl-tRNA synthetase–tRNAPyl structure reveals the molecular basis of orthogonality
Nozawa K, O’Donoghue P, Gundllapalli S, Araiso Y, Ishitani R, Umehara T, Söll D, Nureki O. Pyrrolysyl-tRNA synthetase–tRNAPyl structure reveals the molecular basis of orthogonality. Nature 2008, 457: 1163-1167. PMID: 19118381, PMCID: PMC2648862, DOI: 10.1038/nature07611.Peer-Reviewed Original ResearchConceptsAmino acidsMolecular basisLast universal common ancestorUniversal common ancestorUAG stop codonProteinogenic amino acidsCommon ancestorSuppressor tRNAStop codonDesulfitobacterium hafnienseStandard amino acidsTRNADistinct interactionsProteinPyrrolysinePylRSSelenocysteineAncestorCodonMachineryAcidVivoPairs
2006
Aminoacyl‐tRNAs: Deciphering and Defining the Genetic Message
Ambrogelly A, Salazar J, Sheppard K, Polycarpo C, Oshikane H, Nakamura Y, Fukai S, Nureki O, Söll D. Aminoacyl‐tRNAs: Deciphering and Defining the Genetic Message. 2006, 207-215. DOI: 10.1002/9780470750865.ch18.Peer-Reviewed Original Research
2001
Protein synthesis: Twenty three amino acids and counting
Ibba M, Stathopoulos C, Söll D. Protein synthesis: Twenty three amino acids and counting. Current Biology 2001, 11: r563-r565. PMID: 11509255, DOI: 10.1016/s0960-9822(01)00344-x.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 ResearchConceptsAminoacyl-tRNA synthesisAmino acidsAminoacyl-tRNA synthetaseEvolutionary facetsWhole-genome sequencingCorresponding tRNAsGenetic codeGenome sequencingAminoacyl-tRNACorresponding anticodonTRNACurrent knowledgeStructural dataRecent studiesAnticodonDetailed pictureAcidSequencingSynthetaseEditingProofreadingSynthesisTranslationDirect attachment
1994
Glutamyl‐tRNA as an Intermediate in Glutamate Conversions
Verkamp E, Kumar A, Lloyd A, Martins O, Stange‐Thomann N, Söll D. Glutamyl‐tRNA as an Intermediate in Glutamate Conversions. 1994, 545-550. DOI: 10.1128/9781555818333.ch27.Peer-Reviewed Original ResearchNumber of reactionsPorphyrin ringInitial precursorSynthesis of selenocysteineReactionAmino acidsPhotosynthetic reactionsIntermediatesCompoundsChain formationConversionPrecursorsAcidFormationPorphyrinsFirst conversionHemeSynthesisMoleculesGlu-tRNATransamidationConversion of glutamateGlutamyl-tRNARingSelenocysteine
1990
Transfer 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
1971
A Comparative Study of the Interactions of Escherichia coli Leucyl-, Seryl-, and Valyl-Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids
Myers G, Blank H, Söll D. A Comparative Study of the Interactions of Escherichia coli Leucyl-, Seryl-, and Valyl-Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids. Journal Of Biological Chemistry 1971, 246: 4955-4964. PMID: 4936720, DOI: 10.1016/s0021-9258(18)61956-8.Peer-Reviewed Original ResearchConceptsEscherichia coli KSeryl-tRNA synthetaseLeucyl-tRNA synthetaseRibonucleic acidTransfer ribonucleic acidValyl-tRNA synthetaseTRNA recognitionColi KSynthetase-tRNA complexIsoacceptorsAmino acidsEquilibrium binding studiesPing-pong typeTRNASynthetaseEnzymeKm valuesSubstrate inhibitionBasic similaritiesBinding studiesSerylAcidATPSame bufferSequence
1970
The Interaction of Seryl and of Leucyl Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids
Knowles J, Katze J, Konigsberg W, Söll D. The Interaction of Seryl and of Leucyl Transfer Ribonucleic Acid Synthetases with Their Cognate Transfer Ribonucleic Acids. Journal Of Biological Chemistry 1970, 245: 1407-1415. PMID: 4910800, DOI: 10.1016/s0021-9258(18)63251-x.Peer-Reviewed Original ResearchConceptsSeryl-tRNA synthetaseTransfer ribonucleic acidComplex formationTransfer RNA speciesLeucyl-tRNA synthetaseRibonucleic acidRNA speciesCognate tRNAEscherichia coliSynthetaseDensity gradient centrifugationTRNAStable complexesHigh saltGradient centrifugationSpeciesGel filtrationComplexesSerylColiATPEnzymeAcidSerFormation
1967
Studies on polynucleotides LXXV. Specificity of tRNA for codon recognition as studied by the ribosomal binding technique
Söll D, Cherayil J, Bock R. Studies on polynucleotides LXXV. Specificity of tRNA for codon recognition as studied by the ribosomal binding technique. Journal Of Molecular Biology 1967, 29: 97-112. PMID: 4861614, DOI: 10.1016/0022-2836(67)90183-0.Peer-Reviewed Original ResearchConceptsTransfer RNAAmino acidsE. coliIndividual amino acidsCodon recognitionMultiple codonsMultiple speciesRespective amino acidsWobble hypothesisYeast transfer RNAEscherichia coliCodonRNAColiYeastSpeciesBindingRecognition patternsTRNARibosomesThird letterStimulation of bindingTrinucleotideAcidInteresting differences
1966
Specificity of sRNA for recognition of codons as studied by the ribosomal binding technique
Söll D, Jones D, Ohtsuka E, Faulkner R, Lohrmann R, Hayatsu H, Khorana H, Cherayil J, Hampel A, Bock R. Specificity of sRNA for recognition of codons as studied by the ribosomal binding technique. Journal Of Molecular Biology 1966, 19: 556-573. PMID: 5338858, DOI: 10.1016/s0022-2836(66)80023-2.Peer-Reviewed Original Research