The tyrosyl‐tRNA synthetase from Escherichia coli

Abstract

The structural component of the tyrS gene of Escherichia coli, comprising 1269 base pairs, has been fully sequenced by the combined M13/dideoxychain termination approach. The gene has a codon usage pattern which is typical of highly expressed proteins and similar to other Escherichia coli aminoacyl‐tRNA synthetase genes. Peptide purification and sequencing has been used to locate the N‐terminus and to provide confirmation of 95% of the translated protein sequence. This latter yields on M _r of 47 403 for the Escherichia coli tyrosyl‐tRNA synthetase, and reveals considerable homology with the primary structure of the analogous enzyme isolated from Bacillus staerothermophilus.