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ATPase domain of Hsp70 exhibits intrinsic ATP-ADP exchange activity

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ATPase domain of Hsp70 exhibits intrinsic ATP-ADP exchange activity.htm (400bytes)
Date
2006
Author
Mao, Yubin
Deng, Aihua
Qu, Ning
Wu, Xueji
吴学记
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  • 生命科学-已发表论文 [5901]
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Abstract
The chaperone activity of Hsp70 in protein folding and its conformational switching are regulated through the hydrolysis of ATP and the ATP-ADP exchange cycle. It was reported that, in the presence of physiological concentrations of ATP (-5 mM) and ADP (-0.5 mM), Hsp70 catalyzes ATP-ADP exchange through transfer of gamma-phosphate between ATP and ADP, via an autophosphorylated intermediate, whereas it only catalyzes the hydrolysis of ATP in the absence of ADP. To clarify the functional domain of the ATP-ADP exchange activity of Hsp70, we isolated the 44-kD ATPase domain of Hsp70 after limited proteolysis with alpha-chymotrypsin (EC 3.4.21.1). The possibility of ATP-ADP exchange activity of a contaminating nucleoside diphosphate kinase (EC 2.7.4.6) was monitored throughout the experiments. The purified 44-kD ATPase domain exhibited intrinsic ATP-ADP exchange by catalyzing the transfer of gamma-phosphate between ATP and ADP with acid-stable autophosphorylation at Thr204.
Citation
Biochemistry (Moscow) ,Volume 71, Number 11, 1222-1229
URI
http://dx.doi.org/doi:10.1134/S0006297906110071
https://dspace.xmu.edu.cn/handle/2288/10706

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