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Anticodon‐dependent aminoacylation of RNA minisubstrate by lysyl‐tRNA synthetase
Author(s) -
Khvorova A.M.,
Motorin Yu.A.,
Wolfson A.D.,
Gladilin K.L.
Publication year - 1992
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(92)81483-3
Subject(s) - aminoacylation , transfer rna , biochemistry , oligonucleotide , aminoacyl trna synthetase , enzyme , rna , amino acyl trna synthetases , biology , chemistry , microbiology and biotechnology , dna , gene
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 tRNA Lys 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.