Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Inhibition of Citrate Synthase Thermal Aggregation In Vitro by Recombinant Small Heat Shock Proteins

  • Gong, Weina (State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences) ;
  • Yue, Ming (Laboratory of Feed Ecology and Biotechnology, Feed Research Institute, Chinese Academy of Agricultural Sciences) ;
  • Xie, Bingyan (Institute of Vegetables and Flowers, Chinese Academy of Agricultural Sciences) ;
  • Wan, Fanghao (State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences) ;
  • Guo, Jianying (State Key Laboratory for Biology of Plant Diseases and Insect Pests, Institute of Plant Protection, Chinese Academy of Agricultural Sciences)
  • Published : 2009.12.31
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Abstract

Small heat shock proteins (sHSPs) function as molecular chaperones that protect cells against environmental stresses. In the present study, the genes of hsp17.6 and hsp17.7, cytosolic class I sHSPs, were cloned from a tropical plant, Ageratina adenophorum. Their C-terminal domains were highly conserved with those of sHSPs from other plants, indicating the importance of the C-terminal domains for the structure and activity of sHSPs. The recombinant HSP17.6 and HSP17.7 were applied to determine their chaperone function. In vitro, HSP17.6 and HSP17.7 actively participated in the refolding of the model substrate citrate synthase (CS) and effectively prevented the thermal aggregation of CS at $45^{\circ}C$ and the irreversible inactivation of CS at $38^{\circ}C$ at stoichiometric levels. The prior presence of HSP17.7 was assumed to suppress the thermal aggregation of the model substrate CS. Therefore, this report confirms the chaperone activity of HSP17.6 and HSP17.7 and their potential as a protectant for active proteins.

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References

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