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KMID : 0545120090190121628
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Journal of Microbiology and Biotechnology
2009 Volume.19 No. 12 p.1628 ~ p.1634
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Inhibition of Citrate Synthase Thermal Aggregation In Vitro by Recombinant Small Heat Shock Proteins
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Gong Weina
Wan Fanghao
Guo Jianying
Yue Ming
Xie Bingyan
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Abstract
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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 45oC and the irreversible inactivation of CS at 38oC 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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KEYWORD
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Citrate synthase, Escherichia coli, thermal aggregation, small heat shock proteins
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