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<p>Superoxide dismutase (SOD) is found in a variety of organisms, including animals, plants, and microorganisms, and is widely used in medicine, food, and cosmetics. In this study, a novel heat-resistant SOD from <i>Rhodothermus</i> sp. XMH10 (RhSOD) has been found to have no loss of activity at 80&#xa0;°C and exhibit high thermal stability across a temperature range from 20&#xa0;°C to 80&#xa0;°C. Unlike other reported SODs, RhSOD was found to have a unique small α-helix tail at the C-terminus, consisting of 11 amino acid residues. The absence of the C-terminal α-helix tail of RhSOD was shown to reduce its activity and thermal stability at 80&#xa0;°C, suggesting that the C-terminal α-helix tail is crucial for the high thermal stability of RhSOD. Furthermore, the fusion of the C-terminal α-helix tail to the C-terminus of a thermophilic SOD from <i>Anoxybacillus caldiproteolyticus</i> (AcSOD) enhances its thermal stability at 70&#xa0;°C and 80&#xa0;°C. Circular dichroism (CD) spectral analysis further indicated that the C-terminal α-helix tail could improve the α-helix content, thus enhancing the structural stability of AcSOD. Thus, a novel C-terminal α-helix tail was firstly discovered, which could confer significant thermal stability to host proteins. This finding provides a new theoretical basis for the study of protein thermostability mechanism.</p>

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A Novel C-Terminal Small Tail Provides Thermostability of FeSOD Implying a New Mechanism of Protein Heat Resistance

  • 期刊论文

  • 发表日期：

    2025年7月18日

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  • Weina Lu,
  • Zhuo Jiang,
  • Qi Lin,
  • Zhecheng Yang,
  • Yanli Liu,
  • Wenhui Bi,
  • Zhengying You,
  • Caiying Jiang,
  • Qing Sheng,
  • Zuoming Nie

摘要

Superoxide dismutase (SOD) is found in a variety of organisms, including animals, plants, and microorganisms, and is widely used in medicine, food, and cosmetics. In this study, a novel heat-resistant SOD from Rhodothermus sp. XMH10 (RhSOD) has been found to have no loss of activity at 80 °C and exhibit high thermal stability across a temperature range from 20 °C to 80 °C. Unlike other reported SODs, RhSOD was found to have a unique small α-helix tail at the C-terminus, consisting of 11 amino acid residues. The absence of the C-terminal α-helix tail of RhSOD was shown to reduce its activity and thermal stability at 80 °C, suggesting that the C-terminal α-helix tail is crucial for the high thermal stability of RhSOD. Furthermore, the fusion of the C-terminal α-helix tail to the C-terminus of a thermophilic SOD from Anoxybacillus caldiproteolyticus (AcSOD) enhances its thermal stability at 70 °C and 80 °C. Circular dichroism (CD) spectral analysis further indicated that the C-terminal α-helix tail could improve the α-helix content, thus enhancing the structural stability of AcSOD. Thus, a novel C-terminal α-helix tail was firstly discovered, which could confer significant thermal stability to host proteins. This finding provides a new theoretical basis for the study of protein thermostability mechanism.