Lactobacillus reuteri DSM 20016 produces cobalamin-dependent diol dehydratase in metabolosomes and metabolizes 1,2-propanediol by disproportionation.

2.50
Hdl Handle:
http://hdl.handle.net/10033/48353
Title:
Lactobacillus reuteri DSM 20016 produces cobalamin-dependent diol dehydratase in metabolosomes and metabolizes 1,2-propanediol by disproportionation.
Authors:
Sriramulu, Dinesh Diraviam; Liang, Mingzhi; Hernandez-Romero, Diana; Raux-Deery, Evelyne; Lünsdorf, Heinrich; Parsons, Joshua B; Warren, Martin J; Prentice, Michael B
Abstract:
A 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.
Affiliation:
Department of Microbiology, University College Cork, Cork, Ireland.
Citation:
Lactobacillus reuteri DSM 20016 produces cobalamin-dependent diol dehydratase in metabolosomes and metabolizes 1,2-propanediol by disproportionation. 2008, 190 (13):4559-67 J. Bacteriol.
Journal:
Journal of bacteriology
Issue Date:
Jul-2008
URI:
http://hdl.handle.net/10033/48353
DOI:
10.1128/JB.01535-07
PubMed ID:
18469107
Type:
Article
Language:
en
ISSN:
1098-5530
Appears in Collections:
publications of the research group vaccinology and applied microbiology (VAC)

Full metadata record

DC FieldValue Language
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.en
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

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