This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Schnell, S.
Right arrow Articles by Steinman, H. M.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Schnell, S.
Right arrow Articles by Steinman, H. M.

 Previous Article  |  Next Article 

J. Bacteriol., Oct 1995, 5924-5929, Vol 177, No. 20
Copyright © 1995, American Society for Microbiology

Function and stationary-phase induction of periplasmic copper-zinc superoxide dismutase and catalase/peroxidase in Caulobacter crescentus

S Schnell and HM Steinman
Department of Biochemistry, Albert Einstein College of Medicine, Bronx, New York 10461, USA.

Although cytosolic superoxide dismutases (SODs) are widely distributed among bacteria, only a small number of species contain a periplasmic SOD. One of these is Caulobacter crescentus, which has a copper-zinc SOD (CuZnSOD) in the periplasm and an iron SOD (FeSOD) in the cytosol. The function of periplasmic CuZnSOD was studied by characterizing a mutant of C. crescentus with an insertionally inactivated CuZnSOD gene. Wild-type and mutant strains showed identical tolerance to intracellular superoxide. However, in response to extracellular superoxide, the presence of periplasmic CuZnSOD increased survival by as much as 20-fold. This is the first demonstration that periplasmic SOD defends against external superoxide of environmental origin. This result has implications for those bacterial pathogens that contain a CuZnSOD. C. crescentus was shown to contain a single catalase/peroxidase which, like Escherichia coli KatG catalase/peroxidase, is present in both the periplasmic and cytoplasmic fractions. The growth stage dependence of C. crescentus catalase/peroxidase and SOD activity was studied. Although FeSOD activity was identical in exponential- and stationary-phase cultures, CuZnSOD was induced nearly 4-fold in stationary phase and the catalase/peroxidase was induced nearly 100-fold. Induction of antioxidant enzymes in the periplasm of C. crescentus appears to be an important attribute of the stationary-phase response and may be a useful tool for studying its regulation.


This article has been cited by other articles:

  • Melillo, A. A., Mahawar, M., Sellati, T. J., Malik, M., Metzger, D. W., Melendez, J. A., Bakshi, C. S. (2009). Identification of Francisella tularensis Live Vaccine Strain CuZn Superoxide Dismutase as Critical for Resistance to Extracellularly Generated Reactive Oxygen Species. J. Bacteriol. 191: 6447-6456 [Abstract] [Full Text]  
  • Keith, K. E., Killip, L., He, P., Moran, G. R., Valvano, M. A. (2007). Burkholderia cenocepacia C5424 Produces a Pigment with Antioxidant Properties Using a Homogentisate Intermediate. J. Bacteriol. 189: 9057-9065 [Abstract] [Full Text]  
  • Alvarez-Martinez, C. E., Baldini, R. L., Gomes, S. L. (2006). A Caulobacter crescentus Extracytoplasmic Function Sigma Factor Mediating the Response to Oxidative Stress in Stationary Phase.. J. Bacteriol. 188: 1835-1846 [Abstract] [Full Text]  
  • Hu, P., Brodie, E. L., Suzuki, Y., McAdams, H. H., Andersen, G. L. (2005). Whole-Genome Transcriptional Analysis of Heavy Metal Stresses in Caulobacter crescentus. J. Bacteriol. 187: 8437-8449 [Abstract] [Full Text]  
  • Gee, J. M., Valderas, M. W., Kovach, M. E., Grippe, V. K., Robertson, G. T., Ng, W.-L., Richardson, J. M., Winkler, M. E., Roop, R. M. II (2005). The Brucella abortus Cu,Zn Superoxide Dismutase Is Required for Optimal Resistance to Oxidative Killing by Murine Macrophages and Wild-Type Virulence in Experimentally Infected Mice. Infect. Immun. 73: 2873-2880 [Abstract] [Full Text]  
  • Plewes, K. A., Barr, S. D., Gedamu, L. (2003). Iron Superoxide Dismutases Targeted to the Glycosomes of Leishmania chagasi Are Important for Survival. Infect. Immun. 71: 5910-5920 [Abstract] [Full Text]  
  • Fournier, M., Zhang, Y., Wildschut, J. D., Dolla, A., Voordouw, J. K., Schriemer, D. C., Voordouw, G. (2003). Function of Oxygen Resistance Proteins in the Anaerobic, Sulfate-Reducing Bacterium Desulfovibrio vulgaris Hildenborough. J. Bacteriol. 185: 71-79 [Abstract] [Full Text]  
  • Bong, C. T. H., Fortney, K. R., Katz, B. P., Hood, A. F., Mateo, L. R. S., Kawula, T. H., Spinola, S. M. (2002). A Superoxide Dismutase C Mutant of Haemophilus ducreyi Is Virulent in Human Volunteers. Infect. Immun. 70: 1367-1371 [Abstract] [Full Text]  
  • Folcher, M., Gaillard, H., Nguyen, L. T., Nguyen, K. T., Lacroix, P., Bamas-Jacques, N., Rinkel, M., Thompson, C. J. (2001). Pleiotropic Functions of a Streptomyces pristinaespiralis Autoregulator Receptor in Development, Antibiotic Biosynthesis, and Expression of a Superoxide Dismutase. J. Biol. Chem. 276: 44297-44306 [Abstract] [Full Text]  
  • Dussurget, O., Stewart, G., Neyrolles, O., Pescher, P., Young, D., Marchal, G. (2001). Role of Mycobacterium tuberculosis Copper-Zinc Superoxide Dismutase. Infect. Immun. 69: 529-533 [Abstract] [Full Text]  
  • Lefebre, M. D., Valvano, M. A. (2001). In vitro resistance of Burkholderia cepacia complex isolates to reactive oxygen species in relation to catalase and superoxide dismutase production. Microbiology 147: 97-109 [Abstract] [Full Text]  
  • Kim, J.-a, Sha, Z., Mayfield, J. E. (2000). Regulation of Brucella abortus Catalase. Infect. Immun. 68: 3861-3866 [Abstract] [Full Text]  
  • Battistoni, A., Pacello, F., Folcarelli, S., Ajello, M., Donnarumma, G., Greco, R., Grazia Ammendolia, M., Touati, D., Rotilio, G., Valenti, P. (2000). Increased Expression of Periplasmic Cu,Zn Superoxide Dismutase Enhances Survival of Escherichia coli Invasive Strains within Nonphagocytic Cells. Infect. Immun. 68: 30-37 [Abstract] [Full Text]  
  • Rava, P. S., Somma, L., Steinman, H. M. (1999). Identification of a Regulator That Controls Stationary-Phase Expression of Catalase-Peroxidase in Caulobacter crescentus. J. Bacteriol. 181: 6152-6159 [Abstract] [Full Text]  
  • Mulder, M. A., Zappe, H., Steyn, L. M. (1999). The Mycobacterium tuberculosis katG promoter region contains a novel upstream activator. Microbiology 145: 2507-2518 [Abstract] [Full Text]  
  • Fang, F. C., DeGroote, M. A., Foster, J. W., Baumler, A. J., Ochsner, U., Testerman, T., Bearson, S., Giard, J.-C., Xu, Y., Campbell, G., Laessig, T. (1999). Virulent Salmonella typhimurium has two periplasmic Cu, Zn-superoxide dismutases. Proc. Natl. Acad. Sci. USA 96: 7502-7507 [Abstract] [Full Text]  
  • Kim, E.-J., Chung, H.-J., Suh, B., Hah, Y. C., Roe, J.-H. (1998). Expression and Regulation of the sodF Gene Encoding Iron- and Zinc-Containing Superoxide Dismutase in Streptomyces coelicolor Muller. J. Bacteriol. 180: 2014-2020 [Abstract] [Full Text]  
  • Wilks, K. E., Dunn, K. L. R., Farrant, J. L., Reddin, K. M., Gorringe, A. R., Langford, P. R., Kroll, J. S. (1998). Periplasmic Superoxide Dismutase in Meningococcal Pathogenicity. Infect. Immun. 66: 213-217 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»