Work

Anticodon‐dependent aminoacylation of RNA minisubstrate by lysyl‐tRNA synthetase

Year: 1992

Type: 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.

Source: FEBS Letters

DOI: 10.1016/0014-5793(92)81483-3

Authors: A.M. Khvorova, Yu.A. Motorin, A.D. Wolfson, K.L. Gladilin

Institution: Russian Academy of Sciences

Language: English

Topic: RNA and protein synthesis mechanisms

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: bronze

OpenAlex ID: W2017149904

FWCI: 0.89

Cites: 15

Cited by: 16

Related to: 10