Biopolymers and cell. 2000; 16 (4): 275 - 280

Site-directed mutagenesis of lysine residues located in the connection peptide of the nucleotide-binding domain (Rossman fold) of tyrosyl-tRNA synthetase from bovine liver

V. G. Naidenov, M. I. Vudmaska, A. I. Kortielyuk, G. KJi Matauka

The functional role of lysine 146 and 147 residues located in the connection peptide of the nucleotide-binding domain (Rossman fold) of eukaryotic tyrosyl-tRNA synthetase has been studied by means of site-directed mutagenesis. Replacement of both positively charged residues with asparagine and tyrosine correspondingly as well as substitution of lysine 147 alone cause inactivating of tyrosyl-tRNA synthetase in the reaction of aminoacylation of homologous tRNA. The significance of lysine 147 in stabilization of complex between synthetase and tRNA acceptor stem has been suggested.