ArticleApplied and environmental microbiology2004
Effect of adaptation to ethanol on cytoplasmic and membrane protein profiles of Oenococcus oeni.
Article in Applied and environmental microbiology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 98 citations in OpenAlex.
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- Genomic Analysis of an Excellent Wine-Making StrainPolish journal of microbiology · 2022Article
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- Ethanol tolerance assessment in recombinant E. coli of ethanol responsive genes from Lactobacillus buchneri NRRL B-30929.World journal of microbiology & biotechnology · 2020Article
- Effect of exogenous proline on the ethanolic tolerance and malolactic performance ofJournal of food science and technology · 2020Article
- Increased ethanol tolerance associated with the pntAB locus of Oenococcus oeni and Lactobacillus buchneri.Journal of industrial microbiology & biotechnology · 2019Article
- Relative expression of stress-related genes during acclimation at low temperature of psychrotrophic Oenococcus oeni strains from Patagonian wine.World journal of microbiology & biotechnology · 2018Article
- Co-generation of ethanol and l-lactic acid from corn stalk under a hybrid process.Biotechnology for biofuels · 2018Article
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- Mapping the Physiological Response ofFrontiers in microbiology · 2018Article
- Formation of Staphylococcus aureus Biofilm in the Presence of Sublethal Concentrations of Disinfectants Studied via a Transcriptomic Analysis Using Transcriptome Sequencing (RNA-seq).Applied and environmental microbiology · 2017Article
- Sub-optimal pH Preadaptation Improves the Survival ofFrontiers in microbiology · 2017Article
- Growth and consumption of L-malic acid in wine-like medium by acclimated and non-acclimated cultures of Patagonian Oenococcus oeni strains.Folia microbiologica · 2016Article
- A structural comparison of Listeria monocytogenes protein chaperones PrsA1 and PrsA2 reveals molecular features required for virulence.Molecular microbiology · 2016Article
- Changes in the Expression of Biofilm-Associated Surface Proteins inBioMed research international · 2016Article
- Transcriptomic and Proteomic Analysis ofFrontiers in microbiology · 2016Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The practical application of commercial malolactic starter cultures of Oenococcus oeni surviving direct inoculation in wine requires insight into mechanisms of ethanol toxicity and of acquired ethanol tolerance in this organism. Therefore, the site-specific location of proteins involved in ethanol adaptation, including cytoplasmic, membrane-associated, and integral membrane proteins, was investigated. Ethanol triggers alterations in protein patterns of O. oeni cells stressed with 12% ethanol for 1 h and those of cells grown in the presence of 8% ethanol. Levels of inosine-5'-monophosphate dehydrogenase and phosphogluconate dehydrogenase, which generate reduced nicotinamide nucleotides, were decreased during growth in the presence of ethanol, while glutathione reductase, which consumes NADPH, was induced, suggesting that maintenance of the redox balance plays an important role in ethanol adaptation. Phosphoenolpyruvate:mannose phosphotransferase system (PTS) components of mannose PTS, including the phosphocarrier protein HPr and EII(Man), were lacking in ethanol-adapted cells, providing strong evidence that mannose PTS is absent in ethanol-adapted cells, and this represents a metabolic advantage to O. oeni cells during malolactic fermentation. In cells grown in the presence of ethanol, a large increase in the number of membrane-associated proteins was observed. Interestingly, two of these proteins, dTDT-glucose-4,6-dehydratase and D-alanine:D-alanine ligase, are known to be involved in cell wall biosynthesis. Using a proteomic approach, we provide evidence for an active ethanol adaptation response of O. oeni at the cytoplasmic and membrane protein levels.
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