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 aminoacylation
1991
[15] Biosynthetic method for introducing unnatural amino acids site-specifically into proteins
Ellman J, Mendel D, Anthony-Cahill S, Noren C, Schultz P. [15] Biosynthetic method for introducing unnatural amino acids site-specifically into proteins. Methods In Enzymology 1991, 202: 301-336. PMID: 1784180, DOI: 10.1016/0076-6879(91)02017-4.Peer-Reviewed Original ResearchConceptsAmber nonsense codonUnnatural amino acids siteUnnatural amino acidsTranscription-translation systemAmino acid sitesSuppressor tRNANonsense codonAmino acidsOligonucleotide-directed mutagenesisBiosynthetic methodsAmber mutationGenetic codeTRNAMutagenized DNACodonProtein synthesisChemical aminoacylationSpecific incorporationProteinMutagenesisAcidAminoacylationDNAMutationsSites
1990
Inaccuracy and the Recognition of †RNA
Rogers M, Soll D. Inaccuracy and the Recognition of †RNA. Progress In Nucleic Acid Research And Molecular Biology 1990, 39: 185-208. PMID: 2247608, DOI: 10.1016/s0079-6603(08)60627-3.Peer-Reviewed Original ResearchConceptsATP-dependent stepNoncognate aminoacyl-tRNAsGlutaminyl-tRNA synthetaseAminoacyl-tRNA synthetasesRecognition of tRNAAmber mutationGlnRAminoacyl-tRNAEditing mechanismTRNAMutantsMischargingCentral roleEnzymeSynthetasesMisaminoacylationSupF.SupFSynthetaseMutationsGlutamineMechanismSuppressionAssays
1986
Nonsense mutation in open reading frame E2 of bovine papillomavirus DNA
DiMaio D. Nonsense mutation in open reading frame E2 of bovine papillomavirus DNA. Journal Of Virology 1986, 57: 475-480. PMID: 3003380, PMCID: PMC252759, DOI: 10.1128/jvi.57.2.475-480.1986.Peer-Reviewed Original ResearchConceptsMutant viral DNAOpen reading frame E2C127 cellsBovine papillomavirus DNAViral DNAGenetic mapping experimentsNonsense mutationMouse C127 cellsSingle base substitution mutationsHost cell genomeFull-length viral DNAFocus-forming activityBase substitution mutationsWild-type DNAAmber mutationCell genomeOncogenic transformationViral ORFsSubstitution mutationsORF E2Mapping experimentsMutant DNATransformation assaysDNABovine papillomavirus
1985
First identification of an amber nonsense mutation in Schizosaccharomyces pombe: major differences in the efficiency of homologous versus heterologous yeast suppressor tRNA genes
Krupp G, Thuriaux P, Willis I, Gamulin V, Söll D. First identification of an amber nonsense mutation in Schizosaccharomyces pombe: major differences in the efficiency of homologous versus heterologous yeast suppressor tRNA genes. Molecular Genetics And Genomics 1985, 201: 82-87. PMID: 3903436, DOI: 10.1007/bf00397990.Peer-Reviewed Original ResearchConceptsS. pombeAmber allelesAmber suppressor allelesFission yeast SchizosaccharomycesS. pombe transformantsAmber suppressor tRNANonsense mutationAmber nonsense mutationsSuppressor tRNA geneTRNA genesFission yeastYeast SchizosaccharomycesSchizosaccharomyces pombeSuppressor allelesTRP1 locusAmber mutationSuppressor tRNAPombeNonsense allelesNorthern analysisNitrosoguanidine mutagenesisOchre alleleGenesFirst identificationTRNASer
1984
Transfer RNA mischarging mediated by a mutant Escherichia coli glutaminyl-tRNA synthetase.
Inokuchi H, Hoben P, Yamao F, Ozeki H, Söll D. Transfer RNA mischarging mediated by a mutant Escherichia coli glutaminyl-tRNA synthetase. Proceedings Of The National Academy Of Sciences Of The United States Of America 1984, 81: 5076-5080. PMID: 6382258, PMCID: PMC391640, DOI: 10.1073/pnas.81.16.5076.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseGlnS geneEscherichia coli glutaminyl-tRNA synthetaseAminoacyl-tRNA synthetase genesEarlier genetic studiesAmber suppressor tRNAWild-type enzymeSynthetase geneTRNA speciesAmber anticodonAmber mutationMutant tRNAsSuppressor tRNAGene productsAltered specificityGln mutantMutant geneTransducing phageEnzyme structureGenetic studiesTRNAGenesMischargingBiochemical meansAminoacylation reaction
1975
Isolation and partial characterization of three Escherichia coli mutants with altered transfer ribonucleic acid methylases
Marinus M, Morris N, Söll D, Kwong T. Isolation and partial characterization of three Escherichia coli mutants with altered transfer ribonucleic acid methylases. Journal Of Bacteriology 1975, 122: 257-265. PMID: 1091626, PMCID: PMC235665, DOI: 10.1128/jb.122.1.257-265.1975.Peer-Reviewed Original ResearchConceptsE. coli genomeEscherichia coli mutantsWild-type cellsEscherichia coli KAbility of RNAColi genomeColi mutantsAmber mutationGenetic lociMutagenized cellsColi KMutant strainMutantsLambda phageTRNAS-adenosylmethioninePartial characterizationGenomeCellsCrude enzymeBiosynthesisMethylasesMethylaseLociRNA
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