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The tyrosyl‐tRNA synthetase from Escherichia coli
Author(s) -
Barker D.G.,
Bruton C.J.,
Winter G.
Publication year - 1982
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(82)80781-3
Subject(s) - escherichia coli , transfer rna , chemistry , biochemistry , escherichia coli proteins , rna , gene
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 .