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Journal of Bacteriology, July 2004, p. 4192-4198, Vol. 186, No. 13
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.13.4192-4198.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Dps Protects Cells against Multiple Stresses during Stationary Phase

Sudha Nair and Steven E. Finkel*

Molecular and Computational Biology Program, Department of Biological Sciences, University of Southern California, Los Angeles, California 90089-1340

Received 2 December 2003/ Accepted 26 March 2004

Dps, the nonspecific DNA-binding protein from starved cells, is the most abundant protein in stationary-phase Escherichia coli. Dps homologs are found throughout the bacteria and in at least one archaeal species. Dps has been shown to protect cells from oxidative stress during exponential-phase growth. During stationary phase, Dps organizes the chromosome into a highly ordered, stable nucleoprotein complex called the biocrystal. We show here that Dps is required for long-term stationary-phase viability under competitive conditions and that dps mutants have altered lag phases compared to wild-type cells. We also show that during stationary phase Dps protects the cell not only from oxidative stress but also from UV and gamma irradiation, iron and copper toxicity, thermal stress, and acid and base shock. The protective roles of Dps are most likely achieved through a combination of functions associated with the protein-DNA binding and chromosome compaction, metal chelation, ferroxidase activity, and regulation of gene expression.

* Corresponding author. Mailing address: Molecular and Computational Biology Program, SHS 172, University of Southern California, Los Angeles, CA 90089. Phone: (213) 821-1498. Fax: (213) 740-8631. E-mail: sfinkel{at}usc.edu.

Journal of Bacteriology, July 2004, p. 4192-4198, Vol. 186, No. 13
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.13.4192-4198.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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