Previous Article | Next Article 
Journal of Bacteriology, April 2006, p. 2865-2874, Vol. 188, No. 8
0021-9193/06/$08.00+0 doi:10.1128/JB.188.8.2865-2874.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
Conserving a Volatile Metabolite: a Role for Carboxysome-Like Organelles in Salmonella enterica
Joseph T. Penrod and
John R. Roth*
Microbiology Section, Division of Biological Sciences, University of California, Davis, Davis, California
Received 23 December 2005/
Accepted 30 January 2006
Salmonellae can use ethanolamine (EA) as a sole source of carbon and nitrogen. This ability is encoded by an operon (eut) containing 17 genes, only 6 of which are required under standard conditions (37°C; pH 7.0). Five of the extra genes (eutM, -N, -L, -K, and -G) become necessary under conditions that favor loss of the volatile intermediate, acetaldehyde, which escapes as a gas during growth on EA and is lost at a higher rate from these mutants. The eutM, -N, -L, and -K genes encode homologues of shell proteins of the carboxysome, an organelle shown (in other organisms) to concentrate CO2. We propose that carboxysome-like organelles help bacteria conserve certain volatile metabolitesCO2 or acetaldehydeperhaps by providing a low-pH compartment. The EutG enzyme converts acetaldehyde to ethanol, which may improve carbon retention by forming acetals; alternatively, EutG may recycle NADH within the carboxysome.
* Corresponding author. Mailing address: Microbiology Section, Division of Biological Sciences, University of California, Davis, Davis, CA. Phone: (530) 752-6679. Fax: (530) 752-7663. E-mail:
jrroth{at}ucdavis.edu.
Journal of Bacteriology, April 2006, p. 2865-2874, Vol. 188, No. 8
0021-9193/06/$08.00+0 doi:10.1128/JB.188.8.2865-2874.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
This article has been cited by other articles:
-
Sagermann, M., Ohtaki, A., Nikolakakis, K.
(2009). Crystal structure of the EutL shell protein of the ethanolamine ammonia lyase microcompartment. Proc. Natl. Acad. Sci. USA
106: 8883-8887
[Abstract]
[Full Text]
-
Del Papa, M. F., Perego, M.
(2008). Ethanolamine Activates a Sensor Histidine Kinase Regulating Its Utilization in Enterococcus faecalis. J. Bacteriol.
190: 7147-7156
[Abstract]
[Full Text]
-
Sriramulu, D. D., Liang, M., Hernandez-Romero, D., Raux-Deery, E., Lunsdorf, H., Parsons, J. B., Warren, M. J., Prentice, M. B.
(2008). Lactobacillus reuteri DSM 20016 Produces Cobalamin-Dependent Diol Dehydratase in Metabolosomes and Metabolizes 1,2-Propanediol by Disproportionation. J. Bacteriol.
190: 4559-4567
[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]
-
Tanaka, S., Kerfeld, C. A., Sawaya, M. R., Cai, F., Heinhorst, S., Cannon, G. C., Yeates, T. O.
(2008). Atomic-Level Models of the Bacterial Carboxysome Shell. Science
319: 1083-1086
[Abstract]
[Full Text]
-
Seedorf, H., Fricke, W. F., Veith, B., Bruggemann, H., Liesegang, H., Strittmatter, A., Miethke, M., Buckel, W., Hinderberger, J., Li, F., Hagemeier, C., Thauer, R. K., Gottschalk, G.
(2008). The genome of Clostridium kluyveri, a strict anaerobe with unique metabolic features. Proc. Natl. Acad. Sci. USA
105: 2128-2133
[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]
-
Grose, J. H., Joss, L., Velick, S. F., Roth, J. R.
(2006). Evidence that feedback inhibition of NAD kinase controls responses to oxidative stress. Proc. Natl. Acad. Sci. USA
103: 7601-7606
[Abstract]
[Full Text]