Construction and expression of diphtheria toxin-encoding gene derivatives in Escherichia coli.
We reported earlier that in the periplasmic space of Escherichia coli, truncated derivatives of diphtheria toxin undergo limited proteolysis [Zdanovsky et al., Mol. Biol. 22 (1988) 1037-1293]. Here, we present data indicating that this proteolysis is reduced in cells bearing a mutation in the degP gene. We have also constructed hybrid genes whose products are not secreted into the periplasm. These hybrid genes were expressed in E. coli from both the pR promoter, controlled by the heat-inducible CI857 repressor, and from the P(lac) promoter, controlled by the IPTG-inducible LacI repressor. The latter system proved to be more productive.