FEBS Letters · 1992 · 16 citations · 13 references
Life SciencesBiochemistryMolecular BiologyEnzymologyProtein TranslationRna ProcessingEnzyme InhibitionRibonucleic Acid (Rna) ChemistryRna ModificationAminoacyl-trna SynthetasesAminoacylation Reaction MechanismRna-rna InteractionsSubstrate Specificity Of Aminoacyl-transfer Ribonucleic Acid Synthetases
Specific inhibition of mammalian lysyl-tRNA synthetase by polyU is shown. Inhibition of the enzyme is dependent on the length of the oligonucleotide, since oligoU molecules with a length of less than 8 residues do not inhibit the aminoacylation, whilst the effect of oligoU molecules with a length of about 30 residues is the same as that of polyU. Inhibition is a result of recognition by the enzyme of the tRNALys anticodon sequence (UUU) coded by polyU. Aminoacylation of the oligoU molecule with attached CCA sequence (G(U)20-CCA) by yeast and mammalian lysyl-tRNA synthetases is demonstrated.
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William H. McClain, K. Foss, Robert A. Jenkins et al. · Proceedings of the National Academy of Sciences · 1990 · 103 citations