ABSTRACT Small heat shock proteins are molecular chaperones that bind and prevent aggregation of nonnative proteins. Oxidative stress is known to induce the expression of the small heat shock proteins in prokaryotes and eukaryotes. However, how cells are protected by the heat shock protein is not clearly understood. Dps, DNA-binding protein from starved cells, that is found in many eubacterial and archaebacterial species, protects cells from oxidative and/or nutrient-limited stress. Dps sequesters and oxidizes Fe2+, which would otherwise lead to production of reactive oxygen species that damage the bacterial chromosome. This review describes small heat shock protein and Dps with specific emphasis on their roles under oxidative stress.
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