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The plasmid F OmpP protease, a homologue of OmpT, as a potential obstacle to E. coli ‐based protein production
Author(s) -
Matsuo Ei-ichi,
Sampei Gen-ichi,
Mizobuchi Kiyoshi,
Ito Koreaki
Publication year - 1999
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/s0014-5793(99)01418-0
Subject(s) - proteolysis , plasmid , escherichia coli , protease , bacterial outer membrane , biology , biochemistry , enterobacteriaceae , endogeny , cleavage (geology) , chemistry , microbiology and biotechnology , enzyme , gene , paleontology , fracture (geology)
OmpT, an outer membrane‐localized protease of Escherichia coli , cleaves a number of exogenous and endogenous proteins during their purification. SecY, an endogenous membrane protein, is a target of this artificial proteolysis in vitro. Here we report that SecY cleavage occurs even in cell extracts from ompT ‐disrupted cells, if they carry an F plasmid derivative. A gene, ompP , on the F plasmid was shown to be responsible for this proteolysis. These results indicate that the absence of an F‐like plasmid should be checked when choosing a host strain for E. coli ‐based protein production.