Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Hsp20, a Small Heat Shock Protein of Deinococcus radiodurans, Confers Tolerance to Hydrogen Peroxide in Escherichia coli

  • Singh, Harinder (Research Division for Biotechnology, Korea Atomic Energy Research Institute) ;
  • Appukuttan, Deepti (Research Division for Biotechnology, Korea Atomic Energy Research Institute) ;
  • Lim, Sangyong (Research Division for Biotechnology, Korea Atomic Energy Research Institute)
  • Received : 2014.03.05
  • Accepted : 2014.04.16
  • Published : 2014.08.28
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Abstract

The present study shows that DR1114 (Hsp20), a small heat shock protein of the radiation-resistant bacterium Deinococcus radiodurans, enhances tolerance to hydrogen peroxide ($H_2O_2$) stress when expressed in Escherichia coli. A protein profile comparison showed that E. coli cells overexpressing D. radiodurans Hsp20 (EC-pHsp20) activated the redox state proteins, thus maintaining redox homeostasis. The cells also showed increased expression of pseudouridine (psi) synthases, which are important to the stability and proper functioning of structural RNA molecules. We found that the D. radiodurans mutant strain, which lacks a psi synthase (DR0896), was more sensitive to $H_2O_2$ stress than wild type. These suggest that an increased expression of proteins involved in the control of redox state homeostasis along with more stable ribosomal function may explain the improved tolerance of EC-pHsp20 to $H_2O_2$ stress.

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References

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