2007
Features of Aminoacyl‐tRNA Synthesis Unique to Archaea
Polycarpo C, Sheppard K, Randau L, Ambrogelly A, Cardoso A, Fukai S, Herring S, Hohn M, Nakamura Y, Oshikane H, Palioura S, Salazar J, Yuan J, Nureki O, Söll D. Features of Aminoacyl‐tRNA Synthesis Unique to Archaea. 2007, 198-208. DOI: 10.1128/9781555815516.ch9.Peer-Reviewed Original ResearchAminoacyl-tRNA synthetasesAmino acidsCognate tRNA speciesCorrect amino acidDomains of lifeAminoacyl-tRNA synthetaseIntron-exon junctionsCorresponding tRNAsNanoarchaeum equitansMethylated thiolsM. jannaschiiMature tRNATRNA speciesGenomic studiesAncient familyBulge motifCysteine synthesisMethanogenic archaeaArchaeaBiosynthetic routeAa-tRNATRNATwo-step pathwayCys-tRNACysSynthetases
2006
Mischarging of M. barkeri tRNAPyl with alanine and serine in vitro
Li D, Polycarpo C, Ambrogelly A, Söll D. Mischarging of M. barkeri tRNAPyl with alanine and serine in vitro. The FASEB Journal 2006, 20: a503-a503. DOI: 10.1096/fasebj.20.4.a503-c.Peer-Reviewed Original ResearchNon-canonical amino acidsSecondary structureCognate tRNA speciesPyrrolysyl-tRNA synthetaseAminoacyl-tRNA synthetaseSimilar secondary structureBovine mitochondriaTRNA speciesAlanine tRNAAnticodon stemAcceptor stemAmino acidsM. barkeriMethanosarcina barkeriSerRSsPyrrolysineMultiple mutationsVariable loopSynthetaseSerineShorter variable loopsSynthetase systemBarkeriAlanineStem
2000
Methanococcus jannaschii Prolyl-Cysteinyl-tRNA Synthetase Possesses Overlapping Amino Acid Binding Sites †
Stathopoulos C, Jacquin-Becker C, Becker H, Li T, Ambrogelly A, Longman R, Söll D. Methanococcus jannaschii Prolyl-Cysteinyl-tRNA Synthetase Possesses Overlapping Amino Acid Binding Sites †. Biochemistry 2000, 40: 46-52. PMID: 11141055, DOI: 10.1021/bi002108x.Peer-Reviewed Original ResearchConceptsAmino acidsTRNA synthetaseProtein translation apparatusCysteinyl-tRNA synthetase activityCognate tRNA speciesSite-directed mutagenesisAmino acid activationAbsence of tRNAAmino acid residuesSynthetase activityTranslation apparatusMethanococcus jannaschiiTRNA speciesCysteine activationUnusual enzymeDifferent amino acidsMutant enzymesCysteine bindingProline bindingProlyl-tRNA synthetase activityAcid residuesAminoacyl-tRNAPosition 103Single enzyme
1991
Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and physical properties.
Pande S, Jahn D, Söll D. Histidine tRNA guanylyltransferase from Saccharomyces cerevisiae. I. Purification and physical properties. Journal Of Biological Chemistry 1991, 266: 22826-22831. PMID: 1660461, DOI: 10.1016/s0021-9258(18)54428-8.Peer-Reviewed Original ResearchConceptsAdditional nucleotidesHistidine tRNA genesPolymin P precipitationTRNA genesSodium dodecyl sulfate-polyacrylamide gel electrophoresisDodecyl sulfate-polyacrylamide gel electrophoresisTRNA speciesSulfate-polyacrylamide gel electrophoresisRate zonal sedimentationHomodimeric structureGuanylyltransferaseRelative molecular weightTRNAATP-agaroseGel filtrationAbolishes activityHistidine tRNANative enzymeGuanosine residuesAcceptor RNAEnzymatic activityUnfractionated tRNAGuanosine substrateZonal sedimentationGel electrophoresis
1990
Expression of the Synechocystis sp. strain PCC 6803 tRNA(Glu) gene provides tRNA for protein and chlorophyll biosynthesis
O'Neill G, Söll D. Expression of the Synechocystis sp. strain PCC 6803 tRNA(Glu) gene provides tRNA for protein and chlorophyll biosynthesis. Journal Of Bacteriology 1990, 172: 6363-6371. PMID: 2121711, PMCID: PMC526821, DOI: 10.1128/jb.172.11.6363-6371.1990.Peer-Reviewed Original ResearchConceptsSynechocystis 6803Synechocystis spFirst anticodon baseStrain PCC 6803Cyanobacterium Synechocystis spTotal tRNA populationAmount of chlorophyllNorthern blot analysisChlorophyll biosynthesisALA biosynthesisPrecursor tRNAsPCC 6803TRNA speciesProtein biosynthesisTRNA populationCellular RNAAminoacylation assaysChlorophyll levelsBiosynthesisAddition of inhibitorsBlot analysisTranslation systemDelta-aminolevulinic acidTRNAChlorophyll
1988
Protein biosynthesis in organelles requires misaminoacylation of tRNA
Schön A, Kannangara C, Cough S, SÖll D. Protein biosynthesis in organelles requires misaminoacylation of tRNA. Nature 1988, 331: 187-190. PMID: 3340166, DOI: 10.1038/331187a0.Peer-Reviewed Original ResearchConceptsProtein biosynthesisOrigin of organellesCrude chloroplast extractAnimal mitochondriaRNA involvementSpecific amidotransferaseTRNA speciesConversion of glutamateBarley chloroplastsChloroplast extractsProtein synthesisTRNAOrganellesSpeciesChloroplastsAminoacylation studiesBiosynthesisAmide donorGlutamineGlnCyanobacteriaAmidotransferaseMisaminoacylationMitochondriaOrganisms
1984
Misaminoacylation by glutaminyl-tRNA synthetase: relaxed specificity in wild-type and mutant enzymes.
Hoben P, Uemura H, Yamao F, Cheung A, Swanson R, Sumner-Smith M, Söll D. Misaminoacylation by glutaminyl-tRNA synthetase: relaxed specificity in wild-type and mutant enzymes. The FASEB Journal 1984, 43: 2972-6. PMID: 6389180.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseMutant enzymesWild-type GlnRSAmino-terminal halfAmino acid sequenceAmino acid changesStructural gene mutationsTranslational controlTRNA speciesRelaxed specificityGene sequencesAcid sequenceGlnRRegulation mechanismAcid changesMonomeric polypeptideAmino acidsEnzymeTRNATyrSynthetaseMutationsGene mutationsGlutamineSequenceMisaminoacylationTransfer 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
1983
Organization and Expression of tRNA Genes in Drosophila Melanogaster
Sharp S, Cooley L, DeFranco D, Dingermann T, Söll D. Organization and Expression of tRNA Genes in Drosophila Melanogaster. Recent Results In Cancer Research 1983, 84: 1-14. PMID: 6405456, DOI: 10.1007/978-3-642-81947-6_1.Peer-Reviewed Original ResearchConceptsProtein-synthesizing machineryCorrect amino acidCognate aminoacyl-tRNA synthetasesAminoacyl-tRNA synthetasesTransfer RNA moleculesSpecific recognition featuresStructure-function relationshipsTRNA genesDrosophila melanogasterTRNA speciesRNA moleculesGeneral structural featuresPolypeptide chainTRNAAmino acidsRegulatory processesUseful moleculesFunctional characteristicsStructural featuresIntegral componentRecognition featuresMelanogasterEfficient recognitionSynthetasesRibosomes
1980
Dimeric tRNA precursors in yeast
Schmidt O, Mao J, Ogden R, Beckmann J, Sakano H, Abelson J, Söll D. Dimeric tRNA precursors in yeast. Nature 1980, 287: 750-752. PMID: 6253814, DOI: 10.1038/287750a0.Peer-Reviewed Original ResearchConceptsDimeric tRNA precursorTRNA precursorsDNA fragmentsYeast tRNA genesDifferent genomic regionsNucleotide sequence analysisTRNA genesSaccharomyces cerevisiae1Xenopus nucleiGenomic regionsSpecific transcriptionTRNA speciesPrecursor RNARNA precursorsTRNA moleculesGene regionSequence analysisGene configurationEnzyme activityGenesMode of expressionFragmentsTranscriptionYeastTRNAAsp
1971
Enzymatic Modification of Transfer RNA
Söll D. Enzymatic Modification of Transfer RNA. Science 1971, 173: 293-299. PMID: 4934576, DOI: 10.1126/science.173.3994.293.Peer-Reviewed Original ResearchConceptsTRNA-modifying enzymesTRNA moleculesTRNA genesTransfer RNAAmino acid biosynthesisParticular tRNA speciesNucleic acid-protein interactionsAminoacyl-tRNA synthetaseSimple selection procedureAmino acid acceptorPrecursor tRNAsActive tRNAMature tRNACellular processesTRNA speciesRegulatory mutantsAcid biosynthesisRNA precursorsProtein factorsIsoacceptor tRNAsDifferent amino acidsNucleotide sequencePolynucleotide levelBiological functionsTRNAThe nucleotide sequence of two leucine tRNA species from Escherichia coli K12
Blank H, Sőll D. The nucleotide sequence of two leucine tRNA species from Escherichia coli K12. Biochemical And Biophysical Research Communications 1971, 43: 1192-1197. PMID: 4936129, DOI: 10.1016/0006-291x(71)90589-4.Peer-Reviewed Original Research
1969
CYTOKININS: DISTRIBUTION IN TRANSFER RNA SPECIES OF Escherichia coli*
Armstrong D, Burrows W, Skoog F, Roy K, Söll D. CYTOKININS: DISTRIBUTION IN TRANSFER RNA SPECIES OF Escherichia coli*. Proceedings Of The National Academy Of Sciences Of The United States Of America 1969, 63: 834-841. PMID: 4899879, PMCID: PMC223528, DOI: 10.1073/pnas.63.3.834.Peer-Reviewed Original Research