Inhibition of Citrate Synthase Thermal Aggregation In Vitro by Recombinant Small Heat Shock Proteins

文献类型： 外文期刊

第一作者： Wan, Fanghao

作者： Wan, Fanghao;Guo, Jianying;Gong Weina;Xie, Bingyan;Yue, Ming

作者机构：

关键词： Citrate synthase;Escherichia coli;small heat shock proteins;thermal aggregation

期刊名称：JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY （ 影响因子：2.351； 五年影响因子：2.65 ）

ISSN： 1017-7825

年卷期： 2009 年 19 卷 12 期

页码：

收录情况： SCI

摘要： 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 degrees C and the irreversible inactivation of CS at 38 degrees 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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