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dc.contributor.authorMao, Yubin
dc.contributor.authorDeng, Aihua
dc.contributor.authorQu, Ning
dc.contributor.authorWu, Xueji
dc.contributor.author吴学记
dc.date.accessioned2011-09-01T01:16:28Z
dc.date.available2011-09-01T01:16:28Z
dc.date.issued2006
dc.identifier.citationBiochemistry (Moscow) ,Volume 71, Number 11, 1222-1229zh_CN
dc.identifier.issn0006-2979
dc.identifier.urihttp://dx.doi.org/doi:10.1134/S0006297906110071
dc.identifier.urihttps://dspace.xmu.edu.cn/handle/2288/10706
dc.description.abstractThe 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.zh_CN
dc.language.isoenzh_CN
dc.publisherMAIK NAUKA/INTERPERIODICA/SPRINGERzh_CN
dc.subjectATP-ADP exchangezh_CN
dc.subjectATPase domainzh_CN
dc.subjectautophosphorylationzh_CN
dc.subjectHsp70zh_CN
dc.titleATPase domain of Hsp70 exhibits intrinsic ATP-ADP exchange activityzh_CN
dc.typeArticlezh_CN


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