Dps protects cells against multiple stresses during stationary phase.
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.
Nair
Sudha
S
Molecular and Computational Biology Program, Department of Biological Sciences, University of Southern California, Los Angeles, California 90089-1340, USA.
Finkel
Steven E
SE
D000222:Adaptation, Physiological; D001426:Bacterial Proteins / Q000502:physiology*; D018920:Coculture Techniques; D003300:Copper / Q000494:pharmacology; D004268:DNA-Binding Proteins / Q000502:physiology*; D004926:Escherichia coli / Q000502:physiology*; D005720:Gamma Rays; D006863:Hydrogen-Ion Concentration; D007501:Iron / Q000494:pharmacology; D018384:Oxidative Stress; D013696:Temperature; D014466:Ultraviolet Rays
D001426:Bacterial Proteins; D004268:DNA-Binding Proteins; C083911:DPS protein, Bacteria; D003300:Copper; D007501:Iron