A MAMMALIAN TRYPTOPHANYL-TRANSFER RNA-SYNTHETASE SHOWS LITTLE HOMOLOGY TO PROKARYOTIC SYNTHETASES BUT NEAR IDENTITY WITH MAMMALIAN PEPTIDE-CHAIN RELEASE FACTOR

作者：GARRET M; PAJOT B; TREZEGUET V; LABOUESSE J; MERLE M; GANDAR JC; BENEDETTO JP; SALLAFRANQUE ML; ALTERIO J; GUEGUEN M; SARGER C; LABOUESSE B; BONNET J

来源：Biochemistry, 1991, 30(31): 7809-7817.

DOI：10.1021/bi00245a021

Determination of the amino acid sequence of beef pancreas tryptophanyl-tRNA synthetase was undertaken through both cDNA and direct peptide sequencing. A full-length cDNA clone containing a 475 amino acid open reading frame was obtained. The molecular mass of the corresponding peptide chain, 53 728 Da, was in agreement with that of beef tryptophanyl-tRNA synthetase, as determined by physicochemical methods (54 kDa). Expression of this clone in Escherichia coli led to tryptophanyl-tRNA synthetase activity in cell extracts. The open reading frame included two sequences analogous to the consensus sequences, HIGH and KMSKS, found in class I aminoacyl-tRNA synthetases. The homology with prokaryotic and yeast mitochondrial tryptophanyl-tRNA synthetases was low and was limited to the regions of the consensus sequences. However, a 90% homology was observed with the recently described rabbit peptide chain release factor (eRF) [Lee et al. (1990) Proc. Natl. Acad. Sci. 87, 3508-3512]. Such a strong homology may reveal a new group of genes deriving from a common ancestor, the products of which could be involved in tRNA aminoacylation (tryptophanyl-tRNA synthetase) or translation termination (eRF).

• 出版日期1991-8-6