PMID:11606188
| Citation |
Tanaka, E, Nemoto, TK and Ono, T (2001) Liberation of the intramolecular interaction as the mechanism of heat-induced activation of HSP90 molecular chaperone. Eur. J. Biochem. 268:5270-7 |
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| Abstract |
The molecular chaperone function of HSP90 is activated under heat-stress conditions. In the present study, we investigated the role of the interactions in the heat-induced activation of HSP90 molecular chaperone. The preceding paper demonstrated two domain-domain interactions of HtpG, an Escherichia coli homologue of mammalian HSP90, i.e. an intra-molecular interaction between the N-terminal and middle domains and an intermolecular one between the middle and C-terminal domains. A bacterial two-hybrid system revealed that the two interactions also existed in human HSP90alpha. Partners of the interaction between the N-terminal and middle domains of human HSP90alpha could, but those between the middle and C-terminal domains could not, be replaced by the domains of HtpG. Thus, the interface between the N-terminal and middle domains is essentially unvaried from bacterial to human members of the HSP90-family proteins. The citrate synthase-binding activity of HtpG at an elevated temperature was solely localized in the N-terminal domain, but HSP90alpha possessed two sites in the N-terminal and other domains. The citrate-synthase-binding activity of the N-terminal domain was suppressed by the association of the middle domain. The complex between the N-terminal and middle domains is labile at elevated temperatures, but the other is stable even at 70 degrees C. Taken together, we propose the liberation of the N-terminal client-binding domain from the middle suppressor domain is involved in the temperature-dependent activation mechanism of HSP90 molecular chaperone. |
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| Keywords |
Animals; Bacterial Proteins; Citrate (si)-Synthase/metabolism; Escherichia coli Proteins/chemistry; Escherichia coli Proteins/genetics; Escherichia coli Proteins/metabolism; HSP90 Heat-Shock Proteins/chemistry; HSP90 Heat-Shock Proteins/genetics; HSP90 Heat-Shock Proteins/metabolism; Hot Temperature; Models, Biological; Protein Binding; Protein Structure, Quaternary; Protein Structure, Tertiary; Recombinant Proteins/chemistry; Recombinant Proteins/metabolism; Swine; Thermodynamics; Two-Hybrid System Techniques |
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