Structural features required for the interaction of the Hsp70 molecular chaperone DnaK with its cochaperone DnaJ

被引:118
作者
Suh, WC
Lu, CZ
Gross, CA
机构
[1] Univ Calif San Francisco, Dept Microbiol, San Francisco, CA 94143 USA
[2] Univ Calif San Francisco, Dept Stomatol, San Francisco, CA 94143 USA
关键词
D O I
10.1074/jbc.274.43.30534
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Hsp70 family members together with their Hsp40 co-chaperones function as molecular chaperones, using an ATP-controlled cycle of polypeptide binding and release to mediate protein folding. Hsp40 plays a key role in the chaperone reaction by stimulating the ATPase activity and activating the substrate binding of Hsp70. We have explored the interaction between the Escherichia coli Hsp70 family member, DnaK, and its cochaperone partner DnaJ. Our data show that the binding of ATP, subsequent conformational changes in DnaK, and DnaJ-stimulated ATP hydrolysis are all required for the formation of a DnaK-DnaJ complex as monitored by Biacore analysis. In addition, our data imply that the interaction of the J-domain with DnaK depends on the substrate binding stale of DnaK.
引用
收藏
页码:30534 / 30539
页数:6
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