PMID: 11606188Oct 19, 2001Paper

Liberation of the intramolecular interaction as the mechanism of heat-induced activation of HSP90 molecular chaperone

European Journal of Biochemistry
E TanakaToshio Ono

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 comple...Continue Reading

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Citations

Mar 19, 2008·Cell Stress & Chaperones·Takeshi KobayakawaTakayuki K Nemoto
Oct 9, 2002·Toxicon : Official Journal of the International Society on Toxinology·N DautinD Ladant
Jan 28, 2006·FEMS Microbiology Reviews·James P BurnieRuth C Matthews
May 20, 2016·Scientific Reports·Ewelina M KrysztofinskaRivka L Isaacson
Aug 22, 2002·The Journal of Biological Chemistry·Shawn VogenYair Argon

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