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Anticodon-dependent aminoacylation of RNA minisubstrate by lysyl-tRNA synthetase
A M Khvorova1, Motorin YuA, A D Wolfson
1A.N. Bakh Institute of Biochemistry, Russian Academy of Sciences, Moscow.
FEBS Letters
|December 21, 1992
Abstract:
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.