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Distinct features of protein folding by the GroEL system from a psychrophilic bacterium, Colwellia psychrerythraea 34H

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Abstract

We investigated the protein folding mechanism of the GroEL system of a psychrophilic bacterium, Colwellia psychrerythraea 34H. The amount of mRNA of the groESL operon of C. psychrerythraea was increased about 6-fold after a temperature upshift from 8 to 18 °C for 30 min, suggesting that this temperature causes heat stress in this bacterium. A σ32-type promoter was found upstream of the groESL, suggesting that the C. psychrerythraea groESL is regulated by the σ32 system, like the groESL in E. coli. The maximum ATPase and CTPase activities of CpGroEL were observed at 45 and 35 °C, respectively, which are much higher than the growth temperatures of C. psychrerythraea. We found that the refolding activity of the CpGroEL system in the presence of ATP is lower than that in the presence of CTP. This suggests that ATP is not the optimum energy source of the CpGroEL system. Analyses for the interaction of CpGroEL–CpGroES revealed that CTP could weaken this interaction, resulting in effective refolding function of the CpGroEL system. From these findings, we consider that the CpGroEL system possesses an energy-saving mechanism for avoiding excess consumption of ATP to ensure growth in a low-temperature environment.

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Abbreviations

Cp:

Colwellia psychrerythraea

Ec:

Escherichia coli

HSP:

Heat shock protein

MDH:

Malate dehydrogenase

SR1:

Single-ring mutant of E. coli GroEL

Oa:

Oleispira antarctica

(His6):

Hexahistidine

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Authors and Affiliations

  1. Cell-Free Science and Technology Research Center, Ehime University, 3 Bunkyo-cho, Matsuyama, 790-8577, Japan

    Seiji Yamauchi & Hidenori Hayashi

  2. Graduate School of Science and Technology, Ehime University, Matsuyama, Japan

    Yuya Ueda & Umihiko Inoue

  3. Department of Chemistry, Faculty of Science, Ehime University, Matsuyama, Japan

    Mika Matsumoto

  4. Satellite Venture Business Laboratory, Ehime University, Matsuyama, Japan

    Hidenori Hayashi

Authors
  1. Seiji Yamauchi
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  2. Yuya Ueda
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  3. Mika Matsumoto
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  4. Umihiko Inoue
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  5. Hidenori Hayashi
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Corresponding author

Correspondence to Hidenori Hayashi.

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Communicated by L. Huang.

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Yamauchi, S., Ueda, Y., Matsumoto, M. et al. Distinct features of protein folding by the GroEL system from a psychrophilic bacterium, Colwellia psychrerythraea 34H. Extremophiles 16, 871–882 (2012). https://doi.org/10.1007/s00792-012-0483-7

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  • DOI: https://doi.org/10.1007/s00792-012-0483-7

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