1994
Recognition in the Glutamine tRNA System: from Structure to Function
Sherman J, Rogers M, Söll D. Recognition in the Glutamine tRNA System: from Structure to Function. 1994, 395-409. DOI: 10.1128/9781555818333.ch19.Peer-Reviewed Original ResearchEscherichia coli glutaminyl-tRNA synthetaseFirst high-resolution crystal structureAccurate protein synthesisProtein-RNA interactionsImportant specificity determinantsProtein-RNA complexesClose evolutionary relationshipE. coli GlnRSGlutaminyl-tRNA synthetaseHigh-resolution crystal structuresGlutamyl-tRNA synthetaseAminoacyl-tRNA synthetasesRecognition of tRNAEvolutionary relationshipsTRNA identity elementsTight recognitionSpecificity determinantsTRNA substratesGlnRBiochemical approachesCognate tRNATRNA systemTRNABiophysical techniquesEnzyme mechanism
1988
Yeast RNase P: catalytic activity and substrate binding are separate functions.
Nichols M, Söll D, Willis I. Yeast RNase P: catalytic activity and substrate binding are separate functions. Proceedings Of The National Academy Of Sciences Of The United States Of America 1988, 85: 1379-1383. PMID: 3278310, PMCID: PMC279774, DOI: 10.1073/pnas.85.5.1379.Peer-Reviewed Original ResearchConceptsPrecursor tRNAsRNase PSubstrate bindingGel retardationCatalytic functionRibonucleoprotein RNase PDistinct sequence preferencesEnzyme catalytic functionRNase P cleavage siteMature tRNARNase P.Catalytic integrityTRNA precursorsRNA moietyRNA componentSequence preferenceTRNATRNA complexProtein componentsAcceptor stemEnzyme mechanismMaximal cleavageSecond nucleotideCleavage siteEnzyme