Literature DB >> 12732516

The ftsH gene of the wine bacterium Oenococcus oeni is involved in protection against environmental stress.

Jean-Paul Bourdineaud1, Benjamin Nehmé, Sonia Tesse, Aline Lonvaud-Funel.   

Abstract

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.

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Year:  2003        PMID: 12732516      PMCID: PMC154493          DOI: 10.1128/AEM.69.5.2512-2520.2003

Source DB:  PubMed          Journal:  Appl Environ Microbiol        ISSN: 0099-2240            Impact factor:   4.792


  19 in total

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Review 2.  AAA proteases: cellular machines for degrading membrane proteins.

Authors:  T Langer
Journal:  Trends Biochem Sci       Date:  2000-05       Impact factor: 13.807

Review 3.  Lactic acid bacteria in the quality improvement and depreciation of wine.

Authors:  A Lonvaud-Funel
Journal:  Antonie Van Leeuwenhoek       Date:  1999 Jul-Nov       Impact factor: 2.271

4.  Topology and subcellular localization of FtsH protein in Escherichia coli.

Authors:  T Tomoyasu; K Yamanaka; K Murata; T Suzaki; P Bouloc; A Kato; H Niki; S Hiraga; T Ogura
Journal:  J Bacteriol       Date:  1993-03       Impact factor: 3.490

5.  The Escherichia coli FtsH protein is a prokaryotic member of a protein family of putative ATPases involved in membrane functions, cell cycle control, and gene expression.

Authors:  T Tomoyasu; T Yuki; S Morimura; H Mori; K Yamanaka; H Niki; S Hiraga; T Ogura
Journal:  J Bacteriol       Date:  1993-03       Impact factor: 3.490

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Authors:  A J Martinez-Murcia; N M Harland; M D Collins
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7.  Involvement of FtsH in protein assembly into and through the membrane. I. Mutations that reduce retention efficiency of a cytoplasmic reporter.

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8.  Degradation of sigma 32, the heat shock regulator in Escherichia coli, is governed by HflB.

Authors:  C Herman; D Thévenet; R D'Ari; P Bouloc
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9.  A Lactococcus lactis gene encodes a membrane protein with putative ATPase activity that is homologous to the essential Escherichia coli ftsH gene product.

Authors:  D Nilsson; A A Lauridsen; T Tomoyasu; T Ogura
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  19 in total

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2.  In Vivo PCR-DGGE analysis of Lactobacillus plantarum and Oenococcus oeni populations in red wine.

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Review 5.  Stress Physiology of Lactic Acid Bacteria.

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7.  Effect of adaptation to ethanol on cytoplasmic and membrane protein profiles of Oenococcus oeni.

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9.  Efficient recovery of whole cell proteins in Oenococcus oeni--a comparison of different extraction protocols for high-throughput malolactic starter applications.

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10.  Identification of pOENI-1 and related plasmids in Oenococcus oeni strains performing the malolactic fermentation in wine.

Authors:  Marion Favier; Eric Bilhère; Aline Lonvaud-Funel; Virginie Moine; Patrick M Lucas
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