The plasmid F OmpP protease, a homologue of OmpT, as a potential obstacle to E. coli-based protein production

FEBS Lett. 1999 Nov 12;461(1-2):6-8. doi: 10.1016/s0014-5793(99)01418-0.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Outer Membrane Proteins / genetics
  • Bacterial Outer Membrane Proteins / metabolism*
  • Bacterial Proteins / metabolism
  • Escherichia coli / enzymology*
  • Escherichia coli / genetics
  • Escherichia coli Proteins*
  • Gene Expression Regulation, Bacterial
  • Genes, Bacterial
  • Hydrolases*
  • Plasmids / metabolism*
  • Recombinant Proteins / metabolism
  • SEC Translocation Channels
  • Serine Endopeptidases / metabolism


  • Bacterial Outer Membrane Proteins
  • Bacterial Proteins
  • Escherichia coli Proteins
  • Recombinant Proteins
  • SEC Translocation Channels
  • SecY protein, E coli
  • OmpX protein, E coli
  • Hydrolases
  • Serine Endopeptidases
  • omptin outer membrane protease