2020
Initiation of Protein Synthesis with Non‐Canonical Amino Acids In Vivo
Tharp J, Ad O, Amikura K, Ward F, Garcia E, Cate J, Schepartz A, Söll D. Initiation of Protein Synthesis with Non‐Canonical Amino Acids In Vivo. Angewandte Chemie 2020, 132: 3146-3150. DOI: 10.1002/ange.201914671.Peer-Reviewed Original ResearchNon-canonical amino acidsDistinct non-canonical amino acidsE. coli translational machineryAmino acidsNon-canonical initiationTRNA fMetTranslational machineryInitiator tRNASynthetic biologyE. coli strainsProtein synthesisDiverse sidechainsColi strainsFMetRemarkable versatilityVivoInitial stepSecond positionGenomeTyrRSTRNARedundant copiesMachineryBiologyPolypeptide
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
1998
Maize 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
1996
Aminoacyl-tRNA Synthetases Optimize Both Cognate tRNA Recognition and Discrimination against Noncognate tRNAs †
Sherman J, Söll D. Aminoacyl-tRNA Synthetases Optimize Both Cognate tRNA Recognition and Discrimination against Noncognate tRNAs †. Biochemistry 1996, 35: 601-607. PMID: 8555233, DOI: 10.1021/bi951602b.Peer-Reviewed Original ResearchConceptsTRNA recognitionNoncognate tRNAsEscherichia coli glutaminyl-tRNA synthetaseWild-type GlnRSGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesNucleic acid interactionsGlutamine tRNAFirst base pairMutational analysisSpecific proteinsTRNAGlnRSequence preferenceMutantsBase pairsAcid interactionsDecreased affinityVivoTRNAGlnAffinitySynthetasesProteinSynthetaseCrystal structure
1994
Transfer RNA in Its Fourth Decade
RajBhandary U, Söll D. Transfer RNA in Its Fourth Decade. 1994, 1-4. DOI: 10.1128/9781555818333.ch1.Peer-Reviewed Original Research
1993
Yeast 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
1992
Competition 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 affinityVivoMisacylationAssaysAnticodonBiosynthesisCompetitionCompetition 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: 1547-1552. PMID: 16617497, PMCID: PMC312236, DOI: 10.1093/nar/20.7.1547.Peer-Reviewed Original ResearchAccuracy 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
1989
Structural Basis for Misaminoacylation by Mutant E. coli Glutaminyl-tRNA Synthetase Enzymes
Perona J, Swanson R, Rould M, Steitz T, Söll D. Structural Basis for Misaminoacylation by Mutant E. coli Glutaminyl-tRNA Synthetase Enzymes. Science 1989, 246: 1152-1154. PMID: 2686030, DOI: 10.1126/science.2686030.Peer-Reviewed Original Research
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 Research
1984
The Schizosaccharomyces pombe sup3‐i suppressor recognizes ochre, but not amber codons in vitro and in vivo.
Hottinger H, Stadelmann B, Pearson D, Frendewey D, Kohli J, Söll D. The Schizosaccharomyces pombe sup3‐i suppressor recognizes ochre, but not amber codons in vitro and in vivo. The EMBO Journal 1984, 3: 423-428. PMID: 6370683, PMCID: PMC557361, DOI: 10.1002/j.1460-2075.1984.tb01823.x.Peer-Reviewed Original ResearchConceptsFission yeast Schizosaccharomyces pombeYeast Schizosaccharomyces pombeUGA termination codonVitro translation assaysReadthrough productS. pombeSchizosaccharomyces pombeNonsense mutantsTermination signalOchre suppressorUGA suppressionTranslation assaysAmber codonTermination codonGlobin mRNASup3PombeT substitutionCodonSuppressorPlasmid DNASchizosaccharomycesMutantsVivoAnticodon