The tyrosyl‐tRNA synthetase from Escherichia coli

FEBS Letters

Barker, D.G.²  Bruton, C.J.¹  Winter, G.³ 

[1] Department of Biochemistry, Imperial College of Science and Technology, London, England;Laboratoire de Biochimie, Institut de Biologie Moléculaire et Cellulaire du Centre National de la Recherche Scientifique, Strasbourg, France;Medical Research Council Laboratory of Molecular Biology, Hills Rd., Cambridge CB2 2QH, England

关键词: Aminoacyl-tRNA synthetase;    M13 cloning;    DNA sequencing;   

DOI  :  10.1016/0014-5793(82)80781-3

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown