OmpT expression and activity increase in response to recombinant chloramphenicol acetyltransferase overexpression and heat shock in E. coli.

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TitleOmpT expression and activity increase in response to recombinant chloramphenicol acetyltransferase overexpression and heat shock in E. coli.
Publication TypeJournal Article
Year of Publication2000
AuthorsGill, RT, DeLisa, MP, Shiloach, M, Holoman, TR, Bentley, WE
JournalJ Mol Microbiol Biotechnol
Volume2
Issue3
Pagination283-9
Date Published2000 Jul
ISSN1464-1801
KeywordsBacterial Outer Membrane Proteins, Chloramphenicol O-Acetyltransferase, Escherichia coli, Escherichia coli Proteins, Heat-Shock Response, Peptide Hydrolases, Porins, Recombinant Proteins
Abstract

The activity of a 35 kDa protease increased in response to induced expression of chloramphenicol acetyltransferase (CAT) in E. coli. This protease was partially purified, extensively characterized, and identified via the use of zymogram gels as the outer membrane protease, OmpT. In experiments targeting the overlap of well-characterized stress responses, OmpT activity was found to increase in response to heat shock but was only minimally affected by amino acid limitation. The largest increase in activity was found after induction of CAT. OmpT expression levels also increased in response to induction of recombinant CAT overexpression and heat shock. This is the first report of increased activity and expression of an outer membrane protease during cytoplasmic overexpression of a recombinant protein.

Alternate JournalJ. Mol. Microbiol. Biotechnol.
PubMed ID10937437