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Hsp20, a Small Heat Shock Protein of Deinococcus radiodurans, Confers Tolerance to Hydrogen Peroxide in Escherichia coliS
Hsp20, a Small Heat Shock Protein of Deinococcus radiodurans, Confers Tolerance to Hydrogen Peroxide in Escherichia coliS
Journal of Microbiology and Biotechnology. 2014. Aug, 24(8): 1118-1122
Copyright © 2014, The Korean Society For Microbiology And Biotechnology
  • Received : March 05, 2014
  • Accepted : April 16, 2014
  • Published : August 30, 2014
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About the Authors
Harinder Singh
Deepti Appukuttan
Sangyong Lim
saylim@kaeri.re.kr

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 2 O 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 2 O 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 2 O 2 stress.
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Acknowledgements
This study was supported by the Nuclear R&D program of the Ministry of Science, ICT & Future Planning (MSIP), Republic of Korea.
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