Skip Navigation



Journal of Biochemistry Advance Access published online on November 5, 2008

Journal of Biochemistry, doi:10.1093/jb/mvn149
This Article
Right arrow Advance Access manuscript (PDF)
Right arrow All Versions of this Article:
145/1/95    most recent
mvn149v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Request Permissions
Google Scholar
Right arrow Articles by Duché, D.
Right arrow Articles by Lloubès, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Duché, D.
Right arrow Articles by Lloubès, R.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© The authors 2008. Published by Oxford University Press on behalf of the Japanese Biochemical Society. All rights reserved.

Immunity protein protects colicin E2 from OmpT protease

Denis Duché*, Mohamed Issouf1 and Roland Lloubès

Laboratoire d’Ingénièrie des Systèmes Macromoléculaires, Institut de Biologie Structurale et Microbiologie, CNRS, 31 Chemin Joseph Aiguier, 13402 Marseille cedex 20, France.

*corresponding author: Dr. Denis Duché, Laboratoire d’Ingénièrie des Systèmes Macromoléculaires, Institut de Biologie Structurale et Microbiologie, CNRS, 31 Chemin Joseph Aiguier, 13402 Marseille cedex 20, France. Phone: 33 04 91 16 45 61, Fax: 33 04 91 71 21 24, e-mail: duche{at}ibsm.cnrs-mrs.fr

Received July 4, 2008; Accepted October 21, 2008


   Abstract

The endonuclease colicin E2 (ColE2), a bacteriocidal protein, and the associated cognate immunity protein (Im2) are released from producing Escherichia coli cells. ColE2 interaction with the target cell outer membrane BtuB protein and Tol import machinery allows the dissociation of Im2 from its colicin at the outer membrane surface. Here, we use in vivo approaches to show that a small amount of ColE2-Im2 protein complex bound to sensitive cells is susceptible to proteolytic cleavage by the outer membrane protease, OmpT. The presence of BtuB is required for ColE-Im2 cleavage by OmpT. The amount of colicin cleaved by OmpT is greatly enhanced when ColE2 is dissociated from Im2. We further demonstrate that OmpT cleaves the C-terminal DNase domain of the toxin. As expected, strains that over-produce OmpT are less susceptible to infection by ColE2 than by ColE2-Im2. Our findings reveal an additional function for the immunity protein beside protection of producing cells against their own colicin in the cytoplasm. Im2 protects ColE2 against OmpT-mediated proteolytic attack.

Key Words: BtuB protein, colicin, OmpT protease, translocation, immunity protein


1Present address: Aquapharm Bio-Discovery Ltd. European Centre for Marine Biotechnology


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?




Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.