2023
Dual incorporation of non-canonical amino acids enables production of post-translationally modified selenoproteins
Morosky P, Comyns C, Nunes L, Chung C, Hoffmann P, Söll D, Vargas-Rodriguez O, Krahn N. Dual incorporation of non-canonical amino acids enables production of post-translationally modified selenoproteins. Frontiers In Molecular Biosciences 2023, 10: 1096261. PMID: 36762212, PMCID: PMC9902344, DOI: 10.3389/fmolb.2023.1096261.Peer-Reviewed Original ResearchPost-translational modificationsGenetic code expansionAmino acidsProtein functionCode expansionNon-canonical amino acidsGenetic code expansion techniqueOrthogonal translation systemSkeletal muscle regenerationSelenoprotein functionCell maintenanceBiosynthesis mechanismGenetic systemSelenocysteine insertionPreferred hostMultiple proteinsBiological processesBiology applicationsProtein positionsStop codonCodon sequenceProtein sitesSelenoproteinsChemical biology applicationsMuscle regeneration
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
2012
The Mechanism of Pre-transfer Editing in Yeast Mitochondrial Threonyl-tRNA Synthetase*
Ling J, Peterson KM, Simonović I, Söll D, Simonović M. The Mechanism of Pre-transfer Editing in Yeast Mitochondrial Threonyl-tRNA Synthetase*. Journal Of Biological Chemistry 2012, 287: 28518-28525. PMID: 22773845, PMCID: PMC3436575, DOI: 10.1074/jbc.m112.372920.Peer-Reviewed Original ResearchConceptsPre-transfer editingThreonyl-tRNA synthetaseHydrolytic water moleculeFundamental biological processesNormal cellular functionAminoacyl-tRNA synthetasesPost-transfer editingPost-transfer editing activityTranslational fidelityAminoacylation siteCellular functionsAminoacylation active siteBiological processesMST1Conformational changesEditing activitySeryl adenylateAmino acidsSpecialized domainsEditingSerineSites 100SynthetaseActive siteAdenylate
2001
Genomics-based identification of targets in pathogenic bacteria for potential therapeutic and diagnostic use
Raczniak G, Ibba M, Söll D. Genomics-based identification of targets in pathogenic bacteria for potential therapeutic and diagnostic use. Toxicology 2001, 160: 181-189. PMID: 11246138, DOI: 10.1016/s0300-483x(00)00454-6.Peer-Reviewed Original ResearchConceptsComplete microbial genome sequencesMicrobial genome sequencesFundamental biological processesPathogen-specific pathwaysAminoacyl-tRNA synthesisGenome sequenceBiochemical approachesMammalian hostsIdentification of targetsBiological processesNumber of pathogensProtein synthesisPharmaceutical exploitationSynthesis pathwayCertain pathwaysNovel targetPathogenic bacteriaEnzyme presentPathwayDiagnostic targetsCell viabilityKey processesGenomicsRecent advancesTarget