Cloning and expression of a gene coding for the prolipoprotein signal peptidase of Escherichia coli

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Abstract
An Escherichia coli mutant, Y815, has a temperature‐sensitive prolipoprotein signal peptidase. IPTG‐induced synthesis of the major outer membrane prolipoprotein (PLP) results in the inhibition of cell growth because of accumulation of PLP in its envelope [J. Bacteriol. (1982) 152, 1163–1168]. The 2000 E. coli strains of Clarke and Carbon's collection were screened for the presence of a plasmid complementing the IPTG‐sensitivity of the growth of Y815. One plasmid, pLC3‐13, complemented the IPTG‐sensitivity. The envelope fraction prepared from Y815 transformed by pLC3‐13 showed high activity of the PLP signal peptidase in vitro at high temperature. A 4 kb AccI fragment subcloned onto plasmid pHY001 was shown to carry the gene for the PLP signal peptidase.