0000000000926061

AUTHOR

Françoise Coucheney

showing 4 related works from this author

A small HSP, Lo18, interacts with the cell membrane and modulates lipid physical state under heat shock conditions in a lactic acid bacterium

2005

International audience; The small heat shock proteins (sHSP) are characterized by a chaperone activity to prevent irreversible protein denaturation. This study deals with the sHSP Lo18 induced by multiple stresses in Oenococcus oeni, a lactic acid bacterium. Using in situ immunocytochemistry and cellular fractionation experiments, we demonstrated the association of Lo18 with the membrane in O. oeni cells submitted to heat shock. The same result was obtained after exposure of cells to ethanol or benzyl alcohol, agents known to have an influence on membranes. For the different stresses, the protein was located on the periphery of the cell at membrane level and was also found within the cytopl…

DiphenylhexatrieneHot TemperatureBiophysicsFluorescence PolarizationBiologyBiochemistryImmunolocalizationSmall HSPCell membraneMembrane Lipids03 medical and health scienceschemistry.chemical_compoundHeat shock proteinMembrane fluiditymedicineMembrane fluidityLipid bilayer030304 developmental biologyOenococcus oeni0303 health sciences030306 microbiologyCell MembraneLipid–protein interactionCell Biologybiology.organism_classificationHeat-Shock Proteins SmallGram-Positive CocciMembranemedicine.anatomical_structure[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologychemistryBiochemistryBiophysicsLipochaperoneLaurdanOenococcus oeni
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Distinct amino acids of  the Oenococcus oeni small heat shock protein Lo18 are essential for damaged protein protection and membrane stabilization

2010

The small heat shock protein (smHsp) Lo18 from lactic acid bacteria Oenococcus oeni reduces in vitro thermal aggregation of proteins and modulates the membrane fluidity of native liposomes. An absence of information relating to the way in which the smHsp demonstrates a stabilizing effect for both proteins and membranes prompted this study. We expressed three Lo18 proteins with amino acid substitutions in Escherichia coli to investigate their ability to prevent E. coli protein aggregation and their capacity to stabilize E. coli whole-cell membranes. Our results showed that the alanine 123 to serine substitution induces a decrease in chaperone activity in denaturated proteins, and that the ty…

chemistry.chemical_classificationbiologyProtein aggregationbiology.organism_classificationMicrobiologyAmino acidBiochemistrychemistryMembrane proteinChaperone (protein)Heat shock proteinGeneticsMembrane fluiditybiology.proteinDenaturation (biochemistry)Molecular BiologyOenococcus oeniFEMS Microbiology Letters
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CtsR is the master regulator of stress response gene expression in Oenococcus oeni.

2005

ABSTRACT Although many stress response genes have been characterized in Oenococcus oeni , little is known about the regulation of stress response in this malolactic bacterium. The expression of eubacterial stress genes is controlled both positively and negatively at the transcriptional level. Overall, negative regulation of heat shock genes appears to be more widespread among gram-positive bacteria. We recently identified an ortholog of the ctsR gene in O. oeni . In Bacillus subtilis , CtsR negatively regulates expression of the clp genes, which belong to the class III family of heat shock genes. The ctsR gene of O. oeni is cotranscribed with the downstream clpC gene. Sequence analysis of t…

ChaperoninsOperonMolecular Sequence DataBiologyMicrobiologyGenome03 medical and health sciencesBacterial ProteinsSigma factorHeat shock proteinOperon[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyGene RegulationPromoter Regions GeneticMolecular BiologyGeneHeat-Shock Proteins030304 developmental biologyRegulator geneOenococcus oeniGeneticsRegulation of gene expressionAdenosine Triphosphatases0303 health sciencesBase Sequence030306 microbiologyCTSRGene Expression Regulation Bacterialbiology.organism_classificationDNA-Binding ProteinsGram-Positive CocciRepressor ProteinsMutagenesis Site-DirectedOenococcus oeniGenome BacterialHeat-Shock ResponseBacillus subtilisMolecular ChaperonesJournal of bacteriology
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A new approach for selection of Oenococcus oeni strains in order to produce malolactic starters.

2005

The lactic acid bacterium Oenococcus oeni, mainly responsible for malolactic fermentation (MLF), is used in new winery process as starter culture for direct inoculation. The difficulty to master MLF according to the wine led us to search a new approach to select effective O. oeni strains. Biochemical and molecular tests were performed in order to characterize three strains of O. oeni selected for malolactic starter elaboration. Malolactic and ATPase activities that appeared as a great interest in MLF were measured and the expression of a small heat shock protein Lo18 was evaluated by immunoblotting and real-time PCR. These results were correlated with the performances of strains in two red …

Blotting WesternMalatesWineBiologyMicrobiologyPolymerase Chain ReactionStarterMalolactic fermentationFood microbiologyLactic AcidHeat-Shock ProteinsOenococcus oeniWineAdenosine TriphosphatasesStrain (chemistry)food and beveragesGeneral MedicineHydrogen-Ion Concentrationbiology.organism_classificationKineticsBiochemistryFermentationFood MicrobiologyFermentationBacteriaLeuconostocFood ScienceInternational journal of food microbiology
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