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PMID: 2403549 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

In vivo degradation of secreted fusion proteins by the Escherichia coli outer membrane protease OmpT.

Journal of bacteriology ·Vol. 172 ·No. 1 ·1990-01-00 ·Pages 491-4

Baneyx F, Georgiou G

Abstract

The Escherichia coli outer membrane protease OmpT (protease VII) has been shown to degrade several proteins in vitro, but its function in vivo is uncertain. We demonstrate that OmpT participates in the degradation of a fusion protein secreted into the periplasmic space. A strain with mutations in degP (K.L. Strauch and J. Beckwith, Proc. Natl. Acad. Sci. USA 85:1576-1580, 1988) and ompT exhibits a cumulative decrease in protein degradation and should be useful for the expression of proteolytically sensitive secreted proteins.

MeSH Terms
Bacterial Proteins/metabolism Escherichia coli/metabolism Genes, Bacterial Recombinant Fusion Proteins/metabolism Serine Endopeptidases/physiology Staphylococcal Protein A/metabolism beta-Lactamases/metabolism
Chemicals
Bacterial Proteins Recombinant Fusion Proteins Staphylococcal Protein A Serine Endopeptidases omptin outer membrane protease beta-Lactamases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Baneyx F
Department of Chemical Engineering, University of Texas, Austin 78712.
Georgiou G
References (22)
22 references, click to expand
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1990-01-00
Pages
491-4
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC208460
Subset
IM
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