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Updated: Jul 17, 2026

Directed Protein Packaging within Outer Membrane Vesicles from Escherichia coli: Design, Production and Purification
Published on: November 16, 2016
Role of the ompT mutation in stimulated decrease in colony-forming ability due to intracellular protein aggregate
Bun-ichiro Ono1, Hiroko Kimiduka, Masashi Kubota
1Department of Biotechnology, Faculty of Science and Engineering, Ritsumeikan University, Kusatsu, Shiga, Japan. ono@se.ritsumei.ac.jp
Abstract:
Recently we found that the cells of Escherichia coli strain BL21 producing a fusion protein, GST-Sup35NM, show a much more rapid decrease in colony-forming ability in the stationary phase than control cells. In this study, it was found that an extract of the cells producing GST-Sup35NM forms fibrous protein polymers containing GST-Sup35NM. In the course of the study, we realized that strain BL21 carried the ompT mutation. We suspected that the deficiency in OmpT protease was responsible for the observed phenotype. To test this, we introduced the wild-type ompT gene into strain BL21, and found that the transformed cells recovered the wild-type phenotype. We concluded that OmpT protease, though known to localize on the cell surface, is involved in protein quality control within the cell.
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