Tyrosyl-tRNA-synthetase from bovine liver. Functional role of histidine residues
Gnatenko, D.V.; Korneliuk, A.I.; Matsuka, G.K.
Bioorganicheskaia Khimiia 17(8): 1033-1037
1991
ISSN/ISBN: 0132-3423 PMID: 1750832 Document Number: 383536
A specific chemical modification of histidyl residues in tyrosyl-tRNA synthetase by diethyl pyrocarbonate was performed. It is shown that five of sixteen histidyl residues can react with diethyl pyrocarbonate in the native conditions. Modification of two histidyl residues per dimer results in the inactivation of tyrosyl-tRNA synthetase in both steps of the tRNATyr aminoacylation. All substrates protect tyrosyl-tRNA synthetase against inactivation with diethyl pyrocarbonate, the most effective protector being combination of ATP and tyrosine. Histidyl residues of tyrosyl-tRNA synthetase are suggested to be involved in the catalytic mechanism of aminoacylation of tRNATyr.