6533b852fe1ef96bd12ab80e

RESEARCH PRODUCT

Peptidases specific for proline-containing peptides and their unusual peptide-dependent regulation in Oenococcus oeni

D. AtlanFabienne RemizeJean-francois RittJean GuzzoCosette GrandvaletHervé Alexandre

subject

NitrogenPeptideElectrophoretic Mobility Shift AssayBiologyApplied Microbiology and Biotechnology[ CHIM ] Chemical Sciences03 medical and health scienceschemistry.chemical_compoundBiosynthesisGene expressionMalolactic fermentation[CHIM]Chemical SciencesPromoter Regions GeneticChromatography High Pressure LiquidOenococcus030304 developmental biologyOenococcus oeniDNA Primerschemistry.chemical_classification0303 health sciences030306 microbiologyReverse Transcriptase Polymerase Chain ReactionGeneral MedicineSequence Analysis DNAbiology.organism_classificationYeastEnzymechemistryBiochemistryGene Expression RegulationFermentationBiotechnologyPeptide Hydrolases

description

International audience; Growth of the lactic acid bacterium (LAB) Oenococcus oeni, which is involved in malolactic fermentation during the winemaking process, is stimulated by peptides originating from yeast. In this study, we investigated the impact of peptides on O. oeni growth, peptidase activity and the expression of genes encoding the studied peptidases. Low levels of PepN activity and very high levels of PepI activity were observed in O. oeni, whereas levels of PepX activity were intermediate. The level of biosynthesis of these O. oeni peptidases was shown to depend on peptides present in the culture medium. These results were confirmed by transcriptional analyses of putative pep genes. The mechanism of repression by peptides did not involve a CodY-like regulator. Peptides from yeast decrease the levels of enzymatic activity and relative gene expression of O. oeni peptidases. Peptidases specific for proline-containing peptides are important for O. oeni nitrogen metabolism. We report here for the first time that the enzymes involved in the assimilation of proline-containing peptides by O. oeni differ from the well-described proteolytic system of milk LAB. This may reflect a specific adaptation to the wine environment.

10.1111/j.1365-2672.2008.04032.xhttps://hal.univ-reunion.fr/hal-01201608