Anticodon-dependent aminoacylation of RNA minisubstrate by lysyl-tRNA synthetase. |
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| Authors: | K C Duff S M Kelly N C Price J P Bradshaw |
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| Affiliation: | A.N. Bakh Institute of Biochemistry, Russian Academy of Sciences, Moscow. |
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| 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. |
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