2022
Diversification of aminoacyl-tRNA synthetase activities via genomic duplication
Krahn N, Söll D, Vargas-Rodriguez O. Diversification of aminoacyl-tRNA synthetase activities via genomic duplication. Frontiers In Physiology 2022, 13: 983245. PMID: 36060688, PMCID: PMC9437257, DOI: 10.3389/fphys.2022.983245.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsGenomic duplicationSynthetase familyRecent bioinformatic analysisAminoacyl-tRNA synthetase familySynthetic biology applicationsDomains of lifeNew drug targetsAminoacyl-tRNA synthetase activityGene duplicationPhylogenetic diversityEvolutionary eventsGenetic codeBioinformatics analysisImportant bioactive moleculesAdaptive advantageBiological functionsBiological processesBiology applicationsDrug targetsDuplicationAaRSsCatalytic siteSynthetase activityProteinBioactive molecules
2003
Non-canonical Eukaryotic Glutaminyl- and Glutamyl-tRNA Synthetases Form Mitochondrial Aminoacyl-tRNA in Trypanosoma brucei *
Rinehart J, Horn EK, Wei D, Söll D, Schneider A. Non-canonical Eukaryotic Glutaminyl- and Glutamyl-tRNA Synthetases Form Mitochondrial Aminoacyl-tRNA in Trypanosoma brucei *. Journal Of Biological Chemistry 2003, 279: 1161-1166. PMID: 14563839, DOI: 10.1074/jbc.m310100200.Peer-Reviewed Original ResearchConceptsGlutaminyl-tRNA synthetaseGlutamyl-tRNA synthetaseT. bruceiGln-tRNATrypanosoma bruceiInsect stage T. bruceiT. brucei enzymeRespective gene productsAminoacyl-tRNA synthetasesGlutamyl-tRNA synthetase activitySynthetase activityTransamidation pathwayLeishmania mitochondriaBrucei enzymeMitochondrial tRNAsGlu-tRNAProtein biosynthesisAminoacylation experimentsGene productsRNA interferenceTRNABruceiMitochondriaTotal tRNAGlutaminyl
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 enzymeOne Polypeptide with Two Aminoacyl-tRNA Synthetase Activities
Stathopoulos C, Li T, Longman R, Vothknecht U, Becker H, Ibba M, Söll D. One Polypeptide with Two Aminoacyl-tRNA Synthetase Activities. Science 2000, 287: 479-482. PMID: 10642548, DOI: 10.1126/science.287.5452.479.Peer-Reviewed Original ResearchConceptsProlyl-tRNA synthetaseProtein synthesisCysteinyl-tRNA synthetase activityAmino-terminal sequenceSynthetase activityAminoacyl-tRNA synthetase activityCertain archaeaEvolutionary originMethanococcus jannaschiiGenome sequenceSubstrate specificityGenetic analysisSuch organismsMessenger RNARNA synthetasesSynthetaseSequenceArchaeaJannaschiiSynthetasesRNAOrganismsPolypeptideProlylProtein
1997
Glu-tRNAGln amidotransferase: A novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation
Curnow A, Hong K, Yuan R, Kim S, Martins O, Winkler W, Henkin T, Söll D. Glu-tRNAGln amidotransferase: A novel heterotrimeric enzyme required for correct decoding of glutamine codons during translation. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 11819-11826. PMID: 9342321, PMCID: PMC23611, DOI: 10.1073/pnas.94.22.11819.Peer-Reviewed Original ResearchConceptsTranscriptional unitsGln-tRNAGlnGram-positive eubacteriaHeterotrimeric enzymeGlu-tRNAGlnTranslational apparatusHeterotrimeric proteinGlutamine codonB. subtilisAmidotransferaseSynthetase activityOnly pathwayEnzymeGlutamylEssential componentArchaeaTransamidationEubacteriaOperonCyanobacteriaGATCOrganellesCodonGenesGATA