Literature DB >> 17284844

Role of the ompT mutation in stimulated decrease in colony-forming ability due to intracellular protein aggregate formation in Escherichia coli strain BL21.

Bun-ichiro Ono1, Hiroko Kimiduka, Masashi Kubota, Kazuaki Okuno, Masayuki Yabuta.   

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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Year:  2007        PMID: 17284844     DOI: 10.1271/bbb.60541

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN: 0916-8451            Impact factor:   2.043


  3 in total

1.  Protein aggregates: an aging factor involved in cell death.

Authors:  Etienne Maisonneuve; Benjamin Ezraty; Sam Dukan
Journal:  J Bacteriol       Date:  2008-07-11       Impact factor: 3.490

2.  Carbonylated proteins are detectable only in a degradation-resistant aggregate state in Escherichia coli.

Authors:  Etienne Maisonneuve; Laetitia Fraysse; Sabrina Lignon; Laure Capron; Sam Dukan
Journal:  J Bacteriol       Date:  2008-08-08       Impact factor: 3.490

3.  Effects of mutations in yeast prion [PSI+] on amyloid toxicity manifested in Escherichia coli strain BL21.

Authors:  Bun-ichiro Ono; Hiroshi Kawaminami; Hironori Kobayashi; Masashi Kubota; Yoshikazu Murakami
Journal:  Prion       Date:  2008-01-13       Impact factor: 3.931

  3 in total

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