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Molecular Cloning, Expression and Characterization of Oenococcus oeni Priming Glycosyltransferases

dc.rights.licenseopenen_US
hal.structure.identifierUnité de Recherche Oenologie [Villenave d'Ornon] [OENO]
dc.contributor.authorDIMOPOULOU, Maria
hal.structure.identifierUnité de Recherche Oenologie [Villenave d'Ornon] [OENO]
dc.contributor.authorCLAISSE, Olivier
ORCID: 0000-0002-6273-6289
IDREF: 134190726
hal.structure.identifierUnité de Recherche Oenologie [Villenave d'Ornon] [OENO]
dc.contributor.authorDUTILH, Lucie
hal.structure.identifierUnité de Recherche Oenologie [Villenave d'Ornon] [OENO]
dc.contributor.authorMIOT-SERTIER, Cecile
hal.structure.identifierUnité de Recherche Oenologie [Villenave d'Ornon] [OENO]
dc.contributor.authorBALLESTRA, Patricia
hal.structure.identifierUnité de Recherche Oenologie [Villenave d'Ornon] [OENO]
dc.contributor.authorLUCAS, Patrick
IDREF: 166279137
hal.structure.identifierUnité de Recherche Oenologie [Villenave d'Ornon] [OENO]
dc.contributor.authorDOLS-LAFARGUE, Marguerite
dc.date.accessioned2021-04-29T09:08:30Z
dc.date.available2021-04-29T09:08:30Z
dc.date.issued2017-06-30
dc.identifier.issn1073-6085en_US
dc.identifier.urioai:crossref.org:10.1007/s12033-017-0021-z
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/27131
dc.description.abstractEnOenococcus oeni is the main bacterial species that drives malolactic fermentation in wine. Most O. oeni strains produce capsular exopolysaccharides (EPS) that may contribute to protect them in the wine hostile environment. In O. oeni genome sequences, several genes are predicted to encode priming glycosyltransferases (pGTs). These enzymes are essential for EPS formation as they catalyze the first biosynthetic step through the formation of a phosphoanhydride bond between a hexose-1-phosphate and a lipid carrier undecaprenyl phosphate. In many microorganisms, mutations abolishing the pGT activity also abolish the EPS formation. We first made an in silico analysis of all the genes encoding putative pGT over 50 distinct O. oeni genome sequences. Two polyisoprenyl-phosphate-hexose-1-phosphate transferases, WoaA and WobA, and a glycosyltransferase (It3) were particularly examined for their topology and amino acid sequence. Several isoforms of these enzymes were then expressed in E. coli, and their substrate specificity was examined in vitro. The substrate specificity varied depending on the protein isoform examined, and several mutations were shown to abolish WobA activity but not EPS synthesis. Further analysis of woaA and wobA gene expression levels suggests that WoaA could replace the deficient WobA and maintain EPS formation.
dc.language.isoENen_US
dc.sourcecrossref
dc.subject.enExopolysaccharide
dc.subject.enOenococcus oeni
dc.subject.enPriming glycosyltransferase
dc.title.enMolecular Cloning, Expression and Characterization of Oenococcus oeni Priming Glycosyltransferases
dc.title.alternativeMol Biotechnolen_US
dc.typeArticle de revueen_US
dc.identifier.doi10.1007/s12033-017-0021-zen_US
dc.subject.halSciences du Vivant [q-bio]/Biologie végétaleen_US
dc.identifier.pubmed28667570en_US
bordeaux.journalMolecular Biotechnologyen_US
bordeaux.page323-333en_US
bordeaux.volume59en_US
bordeaux.hal.laboratoriesUnité de Recherche Oenologie - EA 4577en_US
bordeaux.issue8en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionINRAEen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
bordeaux.import.sourcedissemin
hal.exportfalse
workflow.import.sourcedissemin
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