This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Havemann, G. D. Articles by Bobik, T. A. Search for Related Content PubMed PubMed Citation Articles by Havemann, G. D. Articles by Bobik, T. A.

 Previous Article  |  Next Article 

Journal of Bacteriology, March 2002, p. 1253-1261, Vol. 184, No. 5
0021-9193/02/$04.00+0     DOI: 10.1128/JB.184.5.1253-1261.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

PduA Is a Shell Protein of Polyhedral Organelles Involved in Coenzyme B₁₂-Dependent Degradation of 1,2-Propanediol in Salmonella enterica Serovar Typhimurium LT2

Department of Microbiology and Cell Science, University of Florida, Gainesville, Florida 32611

Received 14 September 2001/ Accepted 10 December 2001

Salmonella enterica forms polyhedral organelles involved in coenzyme B₁₂-dependent 1,2-propanediol degradation. These organelles are thought to consist of a proteinaceous shell that encases coenzyme B₁₂-dependent diol dehydratase and perhaps other enzymes involved in 1,2-propanediol degradation. The function of these organelles is unknown, and no detailed studies of their structure have been reported. Genes needed for organelle formation and for 1,2-propanediol degradation are located at the 1,2-propanediol utilization (pdu) locus, but the specific genes involved in organelle formation have not been identified. Here, we show that the pduA gene encodes a shell protein required for the formation of polyhedral organelles involved in coenzyme B₁₂-dependent 1,2-propanediol degradation. A His₆-PduA fusion protein was purified from a recombinant Escherichia coli strain and used for the preparation of polyclonal antibodies. The anti-PduA antibodies obtained were partially purified by a subtraction procedure and used to demonstrate that the PduA protein localized to the shell of the polyhedral organelles. In addition, electron microscopy studies established that strains with nonpolar pduA mutations were unable to form organelles. These results show that the pduA gene is essential for organelle formation and indicate that the PduA protein is a structural component of the shell of these organelles. Physiological studies of nonpolar pduA mutants were also conducted. Such mutants grew similarly to the wild-type strain at low concentrations of 1,2-propanediol but exhibited a period of interrupted growth in the presence of higher concentrations of this growth substrate. Growth tests also showed that a nonpolar pduA deletion mutant grew faster than the wild-type strain at low vitamin B₁₂ concentrations. These results suggest that the polyhedral organelles formed by S. enterica during growth on 1,2-propanediol are not involved in the concentration of 1,2-propanediol or coenzyme B₁₂, but are consistent with the hypothesis that these organelles moderate aldehyde production to minimize toxicity.

Florida Agricultural Experiment Station Journal Series no. R-08598.

This article has been cited by other articles:

• Parsons, J. B., Dinesh, S. D., Deery, E., Leech, H. K., Brindley, A. A., Heldt, D., Frank, S., Smales, C. M., Lunsdorf, H., Rambach, A., Gass, M. H., Bleloch, A., McClean, K. J., Munro, A. W., Rigby, S. E. J., Warren, M. J., Prentice, M. B. (2008). Biochemical and Structural Insights into Bacterial Organelle Form and Biogenesis. J. Biol. Chem. 283: 14366-14375 [Abstract] [Full Text]  
• Sampson, E. M., Bobik, T. A. (2008). Microcompartments for B12-Dependent 1,2-Propanediol Degradation Provide Protection from DNA and Cellular Damage by a Reactive Metabolic Intermediate. J. Bacteriol. 190: 2966-2971 [Abstract] [Full Text]  
• Liu, Y., Leal, N. A., Sampson, E. M., Johnson, C. L. V., Havemann, G. D., Bobik, T. A. (2007). PduL Is an Evolutionarily Distinct Phosphotransacylase Involved in B12-Dependent 1,2-Propanediol Degradation by Salmonella enterica Serovar Typhimurium LT2. J. Bacteriol. 189: 1589-1596 [Abstract] [Full Text]  
• Heinhorst, S., Williams, E. B., Cai, F., Murin, C. D., Shively, J. M., Cannon, G. C. (2006). Characterization of the Carboxysomal Carbonic Anhydrase CsoSCA from Halothiobacillus neapolitanus. J. Bacteriol. 188: 8087-8094 [Abstract] [Full Text]  
• Buan, N. R., Escalante-Semerena, J. C. (2006). Purification and Initial Biochemical Characterization of ATP:Cob(I)alamin Adenosyltransferase (EutT) Enzyme of Salmonella enterica. J. Biol. Chem. 281: 16971-16977 [Abstract] [Full Text]  
• Penrod, J. T., Roth, J. R. (2006). Conserving a Volatile Metabolite: a Role for Carboxysome-Like Organelles in Salmonella enterica.. J. Bacteriol. 188: 2865-2874 [Abstract] [Full Text]  
• Nakayama, S.-i., Watanabe, H. (2006). Mechanism of hilA Repression by 1,2-Propanediol Consists of Two Distinct Pathways, One Dependent on and the Other Independent of Catabolic Production of Propionate, in Salmonella enterica Serovar Typhimurium.. J. Bacteriol. 188: 3121-3125 [Abstract] [Full Text]  
• Starai, V. J., Garrity, J., Escalante-Semerena, J. C. (2005). Acetate excretion during growth of Salmonella enterica on ethanolamine requires phosphotransacetylase (EutD) activity, and acetate recapture requires acetyl-CoA synthetase (Acs) and phosphotransacetylase (Pta) activities. Microbiology 151: 3793-3801 [Abstract] [Full Text]  
• Price-Carter, M., Fazzio, T. G., Vallbona, E. I., Roth, J. R. (2005). Polyphosphate Kinase Protects Salmonella enterica from Weak Organic Acid Stress. J. Bacteriol. 187: 3088-3099 [Abstract] [Full Text]  
• Sampson, E. M., Johnson, C. L. V., Bobik, T. A. (2005). Biochemical evidence that the pduS gene encodes a bifunctional cobalamin reductase. Microbiology 151: 1169-1177 [Abstract] [Full Text]  
• Sheppard, D. E., Penrod, J. T., Bobik, T., Kofoid, E., Roth, J. R. (2004). Evidence that a B12-Adenosyl Transferase Is Encoded within the Ethanolamine Operon of Salmonella enterica. J. Bacteriol. 186: 7635-7644 [Abstract] [Full Text]  
• Buan, N. R., Suh, S.-J., Escalante-Semerena, J. C. (2004). The eutT Gene of Salmonella enterica Encodes an Oxygen-Labile, Metal-Containing ATP:Corrinoid Adenosyltransferase Enzyme. J. Bacteriol. 186: 5708-5714 [Abstract] [Full Text]  
• Brinsmade, S. R., Escalante-Semerena, J. C. (2004). The eutD Gene of Salmonella enterica Encodes a Protein with Phosphotransacetylase Enzyme Activity. J. Bacteriol. 186: 1890-1892 [Abstract] [Full Text]  
• So, A. K.-C., Espie, G. S., Williams, E. B., Shively, J. M., Heinhorst, S., Cannon, G. C. (2004). A Novel Evolutionary Lineage of Carbonic Anhydrase ({varepsilon} Class) Is a Component of the Carboxysome Shell. J. Bacteriol. 186: 623-630 [Abstract] [Full Text]  
• Havemann, G. D., Bobik, T. A. (2003). Protein Content of Polyhedral Organelles Involved in Coenzyme B12-Dependent Degradation of 1,2-Propanediol in Salmonella enterica Serovar Typhimurium LT2. J. Bacteriol. 185: 5086-5095 [Abstract] [Full Text]  
• Aldor, I. S., Kim, S.-W., Prather, K. L. J., Keasling, J. D. (2002). Metabolic Engineering of a Novel Propionate-Independent Pathway for the Production of Poly(3-Hydroxybutyrate-co-3-Hydroxyvalerate) in Recombinant Salmonella enterica Serovar Typhimurium. Appl. Environ. Microbiol. 68: 3848-3854 [Abstract] [Full Text]