The molecular mechanism of Hsp100 chaperone inhibition by the prion curing agent guanidinium chloride

Cathleen Zeymer; Nicolas D. Werbeck; Ilme Schlichting; Jochen Reinstein

doi:10.1074/jbc.M112.432583

The molecular mechanism of Hsp100 chaperone inhibition by the prion curing agent guanidinium chloride

Cathleen Zeymer, Nicolas D. Werbeck, Ilme Schlichting, Jochen Reinstein

Max-Planck-Institut für Medizinische Forschung

Research output: Contribution to journal › Article › peer-review

16 Scopus citations

Abstract

Background: Guanidinium chloride (GdmCl) inhibits Hsp100 chaperones and leads to prion curing in yeast. Results: The Gdm ion binds specifically to the N-terminal nucleotide binding domain, interacting primarily with a conserved glutamate and the bound nucleotide. Conclusion: GdmCl affects the catalytic cycle by both interfering with the essential glutamate and modulating nucleotide binding affinities. Significance: The study elucidates the mechanistic role of GdmCl in Hsp100 chaperone inhibition.

Original language	English
Pages (from-to)	7065-7076
Number of pages	12
Journal	Journal of Biological Chemistry
Volume	288
Issue number	10
DOIs	https://doi.org/10.1074/jbc.M112.432583
State	Published - 8 Mar 2013
Externally published	Yes

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abstract = "Background: Guanidinium chloride (GdmCl) inhibits Hsp100 chaperones and leads to prion curing in yeast. Results: The Gdm ion binds specifically to the N-terminal nucleotide binding domain, interacting primarily with a conserved glutamate and the bound nucleotide. Conclusion: GdmCl affects the catalytic cycle by both interfering with the essential glutamate and modulating nucleotide binding affinities. Significance: The study elucidates the mechanistic role of GdmCl in Hsp100 chaperone inhibition.",

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AU - Reinstein, Jochen

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AB - Background: Guanidinium chloride (GdmCl) inhibits Hsp100 chaperones and leads to prion curing in yeast. Results: The Gdm ion binds specifically to the N-terminal nucleotide binding domain, interacting primarily with a conserved glutamate and the bound nucleotide. Conclusion: GdmCl affects the catalytic cycle by both interfering with the essential glutamate and modulating nucleotide binding affinities. Significance: The study elucidates the mechanistic role of GdmCl in Hsp100 chaperone inhibition.

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The molecular mechanism of Hsp100 chaperone inhibition by the prion curing agent guanidinium chloride

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