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dc.contributor.authorSriramulu, Dinesh Diraviam
dc.contributor.authorLiang, Mingzhi
dc.contributor.authorHernandez-Romero, Diana
dc.contributor.authorRaux-Deery, Evelyne
dc.contributor.authorLünsdorf, Heinrich
dc.contributor.authorParsons, Joshua B
dc.contributor.authorWarren, Martin J
dc.contributor.authorPrentice, Michael B
dc.date.accessioned2009-02-03T09:09:46Z
dc.date.available2009-02-03T09:09:46Z
dc.date.issued2008-07
dc.identifier.citationLactobacillus reuteri DSM 20016 produces cobalamin-dependent diol dehydratase in metabolosomes and metabolizes 1,2-propanediol by disproportionation. 2008, 190 (13):4559-67 J. Bacteriol.en
dc.identifier.issn1098-5530
dc.identifier.pmid18469107
dc.identifier.doi10.1128/JB.01535-07
dc.identifier.urihttp://hdl.handle.net/10033/48353
dc.description.abstractA Lactobacillus reuteri strain isolated from sourdough is known to produce the vitamin cobalamin. The organism requires this for glycerol cofermentation by a cobalamin-dependent enzyme, usually termed glycerol dehydratase, in the synthesis of the antimicrobial substance reuterin. We show that the cobalamin-synthesizing capacity of another L. reuteri strain (20016, the type strain, isolated from the human gut and recently sequenced as F275) is genetically and phenotypically linked, as in the Enterobacteriaceae, to the production of a cobalamin-dependent enzyme which is associated with a bacterial microcompartment (metabolosome) and known as diol dehydratase. We show that this enzyme allows L. reuteri to carry out a disproportionation reaction converting 1,2-propanediol to propionate and propanol. The wide distribution of this operon suggests that it is adapted to horizontal transmission between bacteria. However, there are significant genetic and phenotypic differences between the Lactobacillus background and the Enterobacteriaceae. Electron microscopy reveals that the bacterial microcompartment in L. reuteri occupies a smaller percentage of the cytoplasm than in gram-negative bacteria. DNA sequence data show evidence of a regulatory control mechanism different from that in gram-negative bacteria, with the presence of a catabolite-responsive element (CRE) sequence immediately upstream of the pdu operon encoding diol dehydratase and metabolosome structural genes in L. reuteri. The metabolosome-associated diol dehydratase we describe is the only candidate glycerol dehydratase present on inspection of the L. reuteri F275 genome sequence.
dc.language.isoenen
dc.subject.mesh1-Propanolen
dc.subject.meshBacterial Proteinsen
dc.subject.meshElectrophoresis, Polyacrylamide Gelen
dc.subject.meshGlyceraldehydeen
dc.subject.meshLactobacillus reuterien
dc.subject.meshMicroscopy, Electron, Transmissionen
dc.subject.meshModels, Chemicalen
dc.subject.meshMolecular Sequence Dataen
dc.subject.meshOperonen
dc.subject.meshPolymerase Chain Reactionen
dc.subject.meshPropaneen
dc.subject.meshPropanediol Dehydrataseen
dc.subject.meshPropionatesen
dc.subject.meshPropylene Glycolen
dc.subject.meshSequence Analysis, DNAen
dc.subject.meshSpectrometry, Mass, Matrix-Assisted Laser Desorption-Ionizationen
dc.subject.meshVitamin B 12en
dc.titleLactobacillus reuteri DSM 20016 produces cobalamin-dependent diol dehydratase in metabolosomes and metabolizes 1,2-propanediol by disproportionation.en
dc.typeArticleen
dc.contributor.departmentDepartment of Microbiology, University College Cork, Cork, Ireland.en
dc.identifier.journalJournal of bacteriologyen
refterms.dateFOA2018-06-12T23:06:16Z
html.description.abstractA Lactobacillus reuteri strain isolated from sourdough is known to produce the vitamin cobalamin. The organism requires this for glycerol cofermentation by a cobalamin-dependent enzyme, usually termed glycerol dehydratase, in the synthesis of the antimicrobial substance reuterin. We show that the cobalamin-synthesizing capacity of another L. reuteri strain (20016, the type strain, isolated from the human gut and recently sequenced as F275) is genetically and phenotypically linked, as in the Enterobacteriaceae, to the production of a cobalamin-dependent enzyme which is associated with a bacterial microcompartment (metabolosome) and known as diol dehydratase. We show that this enzyme allows L. reuteri to carry out a disproportionation reaction converting 1,2-propanediol to propionate and propanol. The wide distribution of this operon suggests that it is adapted to horizontal transmission between bacteria. However, there are significant genetic and phenotypic differences between the Lactobacillus background and the Enterobacteriaceae. Electron microscopy reveals that the bacterial microcompartment in L. reuteri occupies a smaller percentage of the cytoplasm than in gram-negative bacteria. DNA sequence data show evidence of a regulatory control mechanism different from that in gram-negative bacteria, with the presence of a catabolite-responsive element (CRE) sequence immediately upstream of the pdu operon encoding diol dehydratase and metabolosome structural genes in L. reuteri. The metabolosome-associated diol dehydratase we describe is the only candidate glycerol dehydratase present on inspection of the L. reuteri F275 genome sequence.


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