The plasmid F OmpP protease, a homologue of OmpT, as a potential obstacle to E. coli-based protein production.
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.
Matsuo
E
E
Institute for Virus Research, Kyoto University, Kyoto, Japan.
Sampei
G
G
Mizobuchi
K
K
Ito
K
K
D001425:Bacterial Outer Membrane Proteins / Q000235:genetics / Q000378:metabolism*; D001426:Bacterial Proteins / Q000378:metabolism; D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D029968:Escherichia coli Proteins; D015964:Gene Expression Regulation, Bacterial; D005798:Genes, Bacterial; D006867:Hydrolases; D010957:Plasmids / Q000378:metabolism*; D011994:Recombinant Proteins / Q000378:metabolism; D000069816:SEC Translocation Channels; D012697:Serine Endopeptidases / Q000378:metabolism
D001425:Bacterial Outer Membrane Proteins; D001426:Bacterial Proteins; D029968:Escherichia coli Proteins; D011994:Recombinant Proteins; D000069816:SEC Translocation Channels; C057841:SecY protein, E coli; C482905:OmpX protein, E coli; D006867:Hydrolases; D012697:Serine Endopeptidases; C057840:omptin outer membrane protease