Effect of a Change of Unusual Initiation Codon TTG to ATG by Site-directed Mutagenesis on γ-Glutamylcysteine Synthetase Gene Expression(Microbiology & Fermentation Industry)

概要

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The gene (gsh I) for γ-glutamylcysteine synthetase (GSH I) has an unusual translational initiation codon TTG. By means of a method involving a mismatched primer, this initiation codon, TTG, of the gsh I gene was replaced by the normal ATG. The GSH I activity increased 50% with the conversion. Expression of the fused genes (gsh I: lacZ) under the control of the gsh I initiation (ATG or TTG) was increased to the same level as above. Although the extent was not so remarkable as in the cases of β-galactosidase and adenylatecyclase, we deduced that the translational efficiency of the gsh I gene was affected by the base substitution of the initiation codon, TTG, to ATG.
社団法人日本農芸化学会の論文
1987-04-23