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Mechanism of Hsp104/ClpB inhibition by prion curing Guanidinium hydrochloride

The Saccharomyces cerevisiae AAA+ protein Hsp104 and its Escherichia coli counterpart ClpB cooperate with Hsp70 chaperones to refold aggregated proteins and fragment prion fibrils. Hsp104/ClpB activity is regulated by interaction of the M-domain with the first ATPase domain (AAA-1), controlling ATP...

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Hauptverfasser: Kummer, Eva (VerfasserIn) , Oguchi, Yuki (VerfasserIn) , Seyffer, Fabian (VerfasserIn) , Bukau, Bernd (VerfasserIn) , Mogk, Axel (VerfasserIn)
Dokumenttyp: Article (Journal)
Sprache:Englisch
Veröffentlicht: 14 February 2013
In: FEBS letters
Year: 2013, Jahrgang: 587, Heft: 6, Pages: 810-817
ISSN:1873-3468
DOI:10.1016/j.febslet.2013.02.011
Online-Zugang:Verlag, lizenzpflichtig, Volltext: https://doi.org/10.1016/j.febslet.2013.02.011
Verlag, lizenzpflichtig, Volltext: https://febs.onlinelibrary.wiley.com/doi/abs/10.1016/j.febslet.2013.02.011
Volltext
Verfasserangaben:Eva Kummer, Yuki Oguchi, Fabian Seyffer, Bernd Bukau, Axel Mogk

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520 |a The Saccharomyces cerevisiae AAA+ protein Hsp104 and its Escherichia coli counterpart ClpB cooperate with Hsp70 chaperones to refold aggregated proteins and fragment prion fibrils. Hsp104/ClpB activity is regulated by interaction of the M-domain with the first ATPase domain (AAA-1), controlling ATP turnover and Hsp70 cooperation. Guanidinium hydrochloride (GdnHCl) inhibits Hsp104/ClpB activity, leading to prion curing. We show that GdnHCl binding exerts dual effects on Hsp104/ClpB. First, GdnHCl strengthens M-domain/AAA-1 interaction, stabilizing Hsp104/ClpB in a repressed conformation and abrogating Hsp70 cooperation. Second, GdnHCl inhibits continuous ATP turnover by AAA-1. These findings provide the mechanistic basis for prion curing by GdnHCl. 
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