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

Citation
E. Matsuo et al., The plasmid F OmpP protease, a homologue of OmpT, as a potential obstacle to E-coli-based protein production, FEBS LETTER, 461(1-2), 1999, pp. 6-8
Citations number
29
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
461
Issue
1-2
Year of publication
1999
Pages
6 - 8
Database
ISI
SICI code
0014-5793(19991112)461:1-2<6:TPFOPA>2.0.ZU;2-H
Abstract
OmpT, an outer membrane-localized protease of Escherichia coli, cleaves a n umber of exogenous and endogenous proteins during their purification. SecY, an endogenous membrane protein, is a target of this artificial proteolysis in vitro. Were we report that SecY cleavage occurs even in cell extracts f rom omp T-disrupted cells, if they carry an F plasmid derivative, A gene, o mpP, On the F plasmid was shown to be responsible for this proteolysis. The se results indicate that the absence of an F-like plasmid should be checked when choosing a host strain for E. coli-based protein production. (C) 1999 Federation of European Biochemical Societies.