| Literature DB >> 1281788 |
A M Khvorova1, A D Wolfson, K L Gladilin.
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.Entities:
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Year: 1992 PMID： 1281788 DOI： 10.1016/0014-5793(92)81483-3
Source DB: PubMed Journal: FEBS Lett ISSN： 0014-5793 Impact factor: 4.124