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PMID: 10498708 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

The propanediol utilization (pdu) operon of Salmonella enterica serovar Typhimurium LT2 includes genes necessary for formation of polyhedral organelles involved in coenzyme B(12)-dependent 1, 2-propanediol degradation.

Journal of bacteriology ·Vol. 181 ·No. 19 ·1999-10-00 ·Pages 5967-75

Bobik TA, Havemann GD, Busch RJ, Williams DS, Aldrich HC

Abstract

The propanediol utilization (pdu) operon of Salmonella enterica serovar Typhimurium LT2 contains genes needed for the coenzyme B(12)-dependent catabolism of 1,2-propanediol. Here the completed DNA sequence of the pdu operon is presented. Analyses of previously unpublished pdu DNA sequence substantiated previous studies indicating that the pdu operon was acquired by horizontal gene transfer and allowed the identification of 16 hypothetical genes. This brings the total number of genes in the pdu operon to 21 and the total number of genes at the pdu locus to 23. Of these, six encode proteins of unknown function and are not closely related to sequences of known function found in GenBank. Two encode proteins involved in transport and regulation. Six probably encode enzymes needed for the pathway of 1,2-propanediol degradation. Two encode proteins related to those used for the reactivation of adenosylcobalamin (AdoCbl)-dependent diol dehydratase. Five encode proteins related to those involved in the formation of polyhedral organelles known as carboxysomes, and two encode proteins that appear distantly related to those involved in carboxysome formation. In addition, it is shown that S. enterica forms polyhedral bodies that are involved in the degradation of 1,2-propanediol. Polyhedra are formed during either aerobic or anaerobic growth on propanediol, but not during growth on other carbon sources. Genetic tests demonstrate that genes of the pdu operon are required for polyhedral body formation, and immunoelectron microscopy shows that AdoCbl-dependent diol dehydratase is associated with these polyhedra. This is the first evidence for a B(12)-dependent enzyme associated with a polyhedral body. It is proposed that the polyhedra consist of AdoCbl-dependent diol dehydratase (and perhaps other proteins) encased within a protein shell that is related to the shell of carboxysomes. The specific function of these unusual polyhedral bodies was not determined, but some possibilities are discussed.

MeSH Terms
Cloning, Molecular Cobamides/metabolism Enzyme Activation Genes, Bacterial Models, Genetic Molecular Sequence Data Multigene Family Operon Organelles/enzymology,genetics Propanediol Dehydratase/metabolism Propylene Glycol/metabolism Salmonella enterica/enzymology,genetics,ultrastructure Sequence Analysis, DNA
Chemicals
Cobamides Propylene Glycol Propanediol Dehydratase cobamamide
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Bobik T A
Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611, USA. bobik@micro.ifas.ufl.edu
Havemann G D
Busch R J
Williams D S
Aldrich H C
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
Published
1999-10-00
Pages
5967-75
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC103623
Subset
IM
Grants
NIGMS NIH HHS · GM59486 · United States
Databases
GENBANK
AF026270
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