Premium
Cloning and expression of a gene coding for the prolipoprotein signal peptidase of Escherichia coli
Author(s) -
Yamagata Hideo,
Daishima Kyoko,
Mizushima Shoji
Publication year - 1983
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(83)80600-0
Subject(s) - escherichia coli , cloning (programming) , chemistry , gene , coding region , gene expression , molecular cloning , microbiology and biotechnology , biology , biochemistry , computer science , programming language
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 Acc I fragment subcloned onto plasmid pHY001 was shown to carry the gene for the PLP signal peptidase.