This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow E-mail 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 Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Bourdineaud, J.-P.
Right arrow Articles by Lonvaud-Funel, A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Bourdineaud, J.-P.
Right arrow Articles by Lonvaud-Funel, A.
Agricola
Right arrow Articles by Bourdineaud, J.-P.
Right arrow Articles by Lonvaud-Funel, A.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, May 2003, p. 2512-2520, Vol. 69, No. 5
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.5.2512-2520.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

The ftsH Gene of the Wine Bacterium Oenococcus oeni Is Involved in Protection against Environmental Stress

Jean-Paul Bourdineaud,* Benjamin Nehmé, Sonia Tesse, and Aline Lonvaud-Funel

Faculté d'Oenologie, Université de Bordeaux II, 33405 Talence Cedex, France

Received 30 July 2002/ Accepted 25 January 2003

The wine bacterium Oenococcus oeni has to cope with harsh environmental conditions, including an acidic pH, a high alcoholic content, nonoptimal growth temperatures, and growth-inhibitory compounds such as fatty acids, phenolic acids, and tannins. We describe the characterization and cloning of the O. oeni ftsH gene, encoding a protease belonging to the ATP binding cassette protein superfamily. The O. oeni FtsH protein is closest in sequence similarity to the FtsH homologue of Lactococcus lactis. The O. oeni ftsH gene proved to be stress-responsive, since its expression increased at high temperatures or under osmotic shock. O. oeni FtsH protein function was tested in an Escherichia coli ftsH mutant strain, and consistent with the O. oeni ftsH gene expression pattern, the O. oeni FtsH protein provided protection for the E. coli ftsH mutant against heat shock. O. oeni and Bradyrhizobium japonicum FtsH proteins also triggered E. coli resistance to wine toxicity. Genes homologous to O. oeni ftsH were detected in many other lactic acid bacteria found in wine, suggesting that this type of gene constitutes a well-conserved stress-protective molecular device.

* Corresponding author. Present address: Laboratoire d'Ecophysiologie et Ecotoxicologie des Systèmes Aquatiques, CNRS (UMR EPOC 5805), Université de Bordeaux I, Place du Docteur Peyneau, 33120 Arcachon, France. Phone: (33) 556 223 926. Fax: (33) 556 549 383. E-mail: jp.bourdineaud{at}ecotox.u-bordeaux.fr.

Applied and Environmental Microbiology, May 2003, p. 2512-2520, Vol. 69, No. 5
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.5.2512-2520.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Fiocco, D., Collins, M., Muscariello, L., Hols, P., Kleerebezem, M., Msadek, T., Spano, G. (2009). The Lactobacillus plantarum ftsH Gene Is a Novel Member of the CtsR Stress Response Regulon. J. Bacteriol. 191: 1688-1694 [Abstract] [Full Text]  
  • Dols-Lafargue, M., Lee, H. Y., Le Marrec, C., Heyraud, A., Chambat, G., Lonvaud-Funel, A. (2008). Characterization of gtf, a Glucosyltransferase Gene in the Genomes of Pediococcus parvulus and Oenococcus oeni, Two Bacterial Species Commonly Found in Wine. Appl. Environ. Microbiol. 74: 4079-4090 [Abstract] [Full Text]  
  • Grandvalet, C., Coucheney, F., Beltramo, C., Guzzo, J. (2005). CtsR Is the Master Regulator of Stress Response Gene Expression in Oenococcus oeni. J. Bacteriol. 187: 5614-5623 [Abstract] [Full Text]  


Copyright © 2010 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»