2002
A one‐step method for in vitro production of tRNA transcripts
Korencić D, Söll D, Ambrogelly A. A one‐step method for in vitro production of tRNA transcripts. Nucleic Acids Research 2002, 30: e105-e105. PMID: 12384607, PMCID: PMC137149, DOI: 10.1093/nar/gnf104.Peer-Reviewed Original ResearchConceptsTRNA transcriptsT7 RNA polymeraseLarge-scale plasmid preparationTRNA genesMicrobial genomesTRNA functionsDNA promoterRNA polymeraseRNA moleculesT7 promoterBiochemical characterizationTranscription templateDNA templateNew enzymeTranscriptsLarge oligonucleotidesTranscriptionGood substratePromoterShort oligonucleotidesEnzymatic digestionRapid productionPlasmid preparationsGenomeOligonucleotide
1999
Mutations in a new Arabidopsis cyclophilin disrupt its interaction with protein phosphatase 2A
Jackson K, Söll D. Mutations in a new Arabidopsis cyclophilin disrupt its interaction with protein phosphatase 2A. Molecular Genetics And Genomics 1999, 262: 830-838. PMID: 10628867, DOI: 10.1007/s004380051147.Peer-Reviewed Original ResearchConceptsProtein phosphatase 2APhosphatase 2AHeterotrimeric protein phosphatase 2ARegulatory subunit AProtein phosphatase 2BMultiple signaling pathwaysAuxin transportPhosphatase 2BPP2A activityAntisense transcriptsResponse pathwaysArabidopsis extractsGene productsN-terminusRoot growthSubunit ASignaling pathwaysNovel cyclophilinCyclophilinArabidopsisAltered formsTranscriptsMutationsPathwayEukaryotes
1994
Coexpression of eukaryotic tRNASer and yeast seryl-tRNA synthetase leads to functional amber suppression in Escherichia coli
Weygand-Durasević I, Nalaskowska M, Söll D. Coexpression of eukaryotic tRNASer and yeast seryl-tRNA synthetase leads to functional amber suppression in Escherichia coli. Journal Of Bacteriology 1994, 176: 232-239. PMID: 8282701, PMCID: PMC205035, DOI: 10.1128/jb.176.1.232-239.1994.Peer-Reviewed Original ResearchConceptsSeryl-tRNA synthetaseYeast seryl-tRNA synthetaseEscherichia coliSerine tRNA geneE. coliConservation of determinantsTRNA genesSchizosaccharomyces pombePrimary transcriptPlasmid promoterAmber suppressionTRNA identityFunctional expressionColiCoexpressionSynthetasePombeGenesPromoterSuppressorTranscriptsOrganismsConservationExpressionEfficient suppression
1984
In vivo and in vitro transcription of the Escherichia coli glutaminyl-tRNA synthetase gene.
Cheung A, Söll D. In vivo and in vitro transcription of the Escherichia coli glutaminyl-tRNA synthetase gene. Journal Of Biological Chemistry 1984, 259: 9953-9958. PMID: 6086662, DOI: 10.1016/s0021-9258(17)42791-8.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseGlutaminyl-tRNA synthetase geneTranslation initiation codon AUGInitiation codon AUGPresence of tRNATermination codon UAAGlnS geneTerminator structureTranscription initiationSynthetase geneTranscription initiatesCodons UAARegulatory signalsCodon AUGTermination sitesTranscription productsSequence analysisStructure upstreamStructural regionsTranscriptionGenesTranscriptsSynthetaseMRNAGln
1982
Post-transcriptional nucleotide addition is responsible for the formation of the 5' terminus of histidine tRNA.
Cooley L, Appel B, Söll D. Post-transcriptional nucleotide addition is responsible for the formation of the 5' terminus of histidine tRNA. Proceedings Of The National Academy Of Sciences Of The United States Of America 1982, 79: 6475-6479. PMID: 6292903, PMCID: PMC347149, DOI: 10.1073/pnas.79.21.6475.Peer-Reviewed Original ResearchConceptsMature tRNAHistidine tRNAPrimary transcriptHistidine tRNA genesGuanylate residuePost-transcriptional additionDrosophila Kc cellsTRNA genesDrosophila melanogasterSchizosaccharomyces pombeTRNAs resultsRNA speciesRNase PEukaryotic mRNAsKc cellsRNA precursorsTRNASequence analysisNucleotide additionAdditional nucleotidesPhosphodiester bondGenesNucleotidesMaturation schemeTranscripts19 Nucleotide Modification in RNA
Kline L, Söll D. 19 Nucleotide Modification in RNA. The Enzymes 1982, 15: 567-582. DOI: 10.1016/s1874-6047(08)60291-7.Peer-Reviewed Original ResearchRNA base modificationsAnticodon of tRNAComplex nucleotidesNucleotide modificationsAdenosine modificationsEnzymatic modificationRNA chainsBase modificationsEnzymatic stepsAdenosine residuesUracil residuesNucleotidesRNABiochemical evidenceEnzymeModifying groupUracil nucleotidesResiduesGuanine structureFirst positionTRNAAnticodonGeneticsTranscriptsModification