Biopolym. Cell. 1997; 13(6):474-478.
Structure and Function of Biopolymers
Homology of C-terminal non-catalytic domain of mammalian tyrosyl-tRNA synthetase with cylokine EMAP II and non-catalytic domains of methionyl- and phenylalanyl-tRNA synthetases
1Levanets O. V., 1Naidenov V. G., 1Odynets K. A., 1Woodmaska M. I., 1Matsuka G. Kh., 1Kornelyuk A. I.
- Institute of Molecular Biology and Genetics, NAS of Ukraine
150, Akademika Zabolotnoho Str., Kyiv, Ukraine, 03680
Abstract
Mammalian tyrosyl-tRNA synthetase contains C-terminal domain which is dispensable for the enzyme catalytic activity in the. aminoacylation of homologous tRNATyr. Cloning and sequencing cDNA which encodes this mammalian tyrosyl-tRNA synthetase was performed by the 3'-RACE method. Comparison of the amino acid sequence of the C-terminal domain of this mammalian tyrosyl-tRNA synthetase with other proteins using program BLASTP has shown the highest homology level (62.7 % identity) with a new cytokine, EMAP II, inducible by chemical cancerogenesis and corresponding to the p43 protein from high molecular weight aaRS complex of mammalians and also with non-catalytic C-terminal domains of methionyl-tRNA synthetases from nematode (62.7 %) and bacteria (27.7 %) and with N-terminal domain of the β-subunit of phenylalanyl-tRNA synthetase of E. coli (26.7 %). The hypothesis was proposed about possible forming of isolated C-domain as a result of the proteolytic digestion of tyrosyl-tRNA synthetase by intracellular proteases and about possible cytokinc-like activity of this C-domain.
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