Open AccessTemperature-sensitive processing of outer membrane lipoprotein in an Escherichia coli mutant
Author(s) -
Hideo Yamagata,
C Ippolito,
Masatoshi Inukai,
Masayori Inouye
Publication year - 1982
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.152.3.1163-1168.1982
Subject(s) - mutant , bacterial outer membrane , biology , escherichia coli , signal peptide , signal peptidase , cleavage (geology) , biochemistry , lipoprotein , gene , peptide sequence , cholesterol , paleontology , fracture (geology)
A mutant of Escherichia coli that accumulated prolipoprotein, a secretory precursor of the outer membrane lipoprotein, was isolated. The prolipoprotein accumulated in this mutant was modified by glyceride, but the in vitro cleavage of the signal peptide of the accumulated prolipoprotein was found to be temperature sensitive. The mutation appears to be located outside the gene for the lipoprotein, thus suggesting that the gene for the signal peptidase for the prolipoprotein was mutated.