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 ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesAnti-Bacterial AgentsBorrelia burgdorferi GroupChlamydia InfectionsChlamydia trachomatisEnzyme InhibitorsGenome, BacterialLyme DiseaseProteomeRNA, TransferConceptsComplete 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
1999
Substrate recognition by class I lysyl-tRNA synthetases: A molecular basis for gene displacement
Ibba M, Losey H, Kawarabayasi Y, Kikuchi H, Bunjun S, Söll D. Substrate recognition by class I lysyl-tRNA synthetases: A molecular basis for gene displacement. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 418-423. PMID: 9892648, PMCID: PMC15151, DOI: 10.1073/pnas.96.2.418.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acyl-tRNA SynthetasesBase SequenceBorrelia burgdorferi GroupCloning, MolecularDiphosphatesEscherichia coliEvolution, MolecularGenes, ArchaealGenes, BacterialGenetic Complementation TestKineticsLysine-tRNA LigaseMethanococcusMolecular Sequence DataNucleic Acid ConformationPhylogenyRNA, Transfer, Amino AcylSequence Analysis, DNASubstrate SpecificityTranscription, GeneticConceptsClass II LysRSAminoacyl-tRNA synthetasesLysyl-tRNA synthetasesSubstrate recognitionMolecular basisBacterial class IClass II enzymesSequence-specific recognitionGene displacementTranslational apparatusTRNA recognitionEscherichia coli strainsLysRSLysRSsSame nucleotideSynthetasesDiscriminator baseUnrelated typesLysine activationCertain bacteriaII enzymesColi strainsTRNALysClass IEnzyme
1997
Archaeal-type lysyl-tRNA synthetase in the Lyme disease spirochete Borrelia burgdorferi
Ibba M, Bono J, Rosa P, Söll D. Archaeal-type lysyl-tRNA synthetase in the Lyme disease spirochete Borrelia burgdorferi. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 14383-14388. PMID: 9405621, PMCID: PMC24988, DOI: 10.1073/pnas.94.26.14383.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsArchaeaBorrelia burgdorferiBorrelia burgdorferi GroupHumansLyme DiseaseLysine-tRNA LigaseMolecular Sequence DataPhylogenySequence AlignmentConceptsLysyl-tRNA synthetasesLysyl-tRNA synthetaseOpen reading frameReading frameAminoacyl-tRNA synthetasesLyme disease spirochete Borrelia burgdorferiGroup of enzymesLysyl-tRNA synthetase activityAmino acid levelsBacterial pathogen Borrelia burgdorferiArchaeal kingdomHeterologous expressionProtein biosynthesisGenomic sequencesMRNA translationPathogen Borrelia burgdorferiSignificant similarityLysyl-tRNASynthetasesB. burgdorferiBorrelia burgdorferiEscherichia coliEukaryaSpirochete Borrelia burgdorferiPathogenic spirochetes