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Khvorova AM, Motorin YuA, Wolfson AD, et al. Anticodon-dependent aminoacylation of RNA minisubstrate by lysyl-tRNA synthetase. FEBS Lett. 1992;314(3):256-8doi: 10.1016/0014-5793(92)81483-3.
Khvorova, A. M., Motorin YuA, Wolfson, A. D., & Gladilin, K. L. (1992). Anticodon-dependent aminoacylation of RNA minisubstrate by lysyl-tRNA synthetase. FEBS letters, 314(3), 256-8. https://doi.org/10.1016/0014-5793(92)81483-3
Khvorova, A M, et al. "Anticodon-dependent aminoacylation of RNA minisubstrate by lysyl-tRNA synthetase." FEBS letters vol. 314,3 (1992): 256-8. doi: https://doi.org/10.1016/0014-5793(92)81483-3
Khvorova AM, Motorin YuA, Wolfson AD, Gladilin KL. Anticodon-dependent aminoacylation of RNA minisubstrate by lysyl-tRNA synthetase. FEBS Lett. 1992 Dec 21;314(3):256-8. doi: 10.1016/0014-5793(92)81483-3. PMID: 1281788.
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FEBS Lett. 1992 Dec 21;314(3):256-8. doi: 10.1016/0014-5793(92)81483-3.

Anticodon-dependent aminoacylation of RNA minisubstrate by lysyl-tRNA synthetase.

FEBS letters

A M Khvorova, Motorin YuA, A D Wolfson, K L Gladilin

Affiliations

  1. A.N. Bakh Institute of Biochemistry, Russian Academy of Sciences, Moscow.

PMID: 1281788 DOI: 10.1016/0014-5793(92)81483-3
Free Article

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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