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KMID : 0578320110320030257
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Molecules and Cells
2011 Volume.32 No. 3 p.257 ~ p.264
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Engineering of 2-Cys Peroxiredoxin for Enhanced Stress-Tolerance
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An Byung-Chull
Lee Seung-Sik
Lee Jae-Taek
Wi Seung-Gon
Byung Yeoup
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Abstract
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A typical 2-cysteine peroxiredoxin (2-Cys Prx)-like protein (PpPrx) that alternatively acts as a peroxidase or a mole-cular chaperone in Pseudomonas putida KT2440 was previously characterized. The dual functions of PpPrx are regulated by the existence of an additional Cys112 between the active Cys51 and Cys171 residues. In the present study, additional Cys residues (Cys31, Cys112, and Cys192) were added to PpPrx variants to improve their enzymatic func-tion. The optimal position of the additional Cys residues for the dual functionality was assessed. The peroxidase activities of the S31C and Y192C mutants were increased 3- to 4-fold compared to the wild-type, while the chaperone activity was maintained at > 66% of PpPrx. To investigate whether optimization of the dual functions could enhance stress-tolerance in vivo, a complementation study was performed. The S31C and Y192C mutants showed a much greater tolerance than other variants under a complex condition of heat and oxidative stresses. The optimized dual functions of PpPrx could be adapted for use in bioen-gineering systems and industries, such as to develop or-ganisms that are more resistant to extreme environments.
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KEYWORD
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dual function engineering, dual functions, extreme stress, peroxiredoxin, site-directed mutagenesis
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