Heterologous Expression of Chaperones from Hyperthermophilic Archaea Inhibits Aminoglycoside-Induced Protein Misfolding in Escherichia coli

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S. Peng¹, Z. Chu^2,3, J. Lu^2,3, D. Li^2,3, Y. Wang^1*, S. Yang^2,3, and Y. Zhang^2,3*

¹State Key Laboratory of Bioreactor Engineering, East China University of Science and Technology, 200237 Shanghai, China; E-mail: yhwang@ecust.edu.cn

²Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences, 200031 Shanghai, China; E-mail: yzhang@sibs.ac.cn

³Key Laboratory of Synthetic Biology, Chinese Academy of Sciences, 200032 Shanghai, China

^* To whom correspondence should be addressed.

Received May 17, 2017; Revision received June 13, 2017

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Aminoglycoside antibiotics affect protein translation fidelity and lead to protein aggregation and an increase in intracellular oxidative stress level as well. The overexpression of the chaperonin GroEL/GroES system promotes short-term tolerance to aminoglycosides in Escherichia coli. Here, we demonstrated that the coexpression of prefoldin or Hsp60 originating from the hyperthermophilic archaeon Pyrococcus furiosus in E. coli cells can rescue cell growth and inhibit protein aggregation induced by streptomycin exposure. The results of our study show that hyperthermophilic chaperones endow E. coli with a higher tolerance to streptomycin than the GroEL/GroES system, and that they exert better effects on the reduction of intracellular protein misfolding, indicating that these chaperones have unique features and functions.

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KEY WORDS: aminoglycoside, protein mistranslation, Escherichia coli, hyperthermophilic archaeon, Pyrococcus furiosus, chaperone

DOI: 10.1134/S0006297917100091

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