NDLI: Differences in the Curing of [PSI+ ] Prion by Various Methods of Hsp104 Inactivation

Content Provider	PubMed Central
Author	Park, Yang-nim Morales, David Rubinson, Emily H. Daniel, Masison Eisenberg, Evan Greene, Lois E.
Editor	Tuite, Mick F.
Copyright Year	2012
Abstract	[PSI +] yeast, containing the misfolded amyloid conformation of Sup35 prion, is cured by inactivation of Hsp104. There has been controversy as to whether inactivation of Hsp104 by guanidine treatment or by overexpression of the dominant negative Hsp104 mutant, Hsp104-2KT, cures [PSI +] by the same mechanism– inhibition of the severing of the prion seeds. Using live cell imaging of Sup35-GFP, overexpression of Hsp104-2KT caused the foci to increase in size, then decrease in number, and finally disappear when the cells were cured, similar to that observed in cells cured by depletion of Hsp104. In contrast, guanidine initially caused an increase in foci size but then the foci disappeared before the cells were cured. By starving the yeast to make the foci visible in cells grown with guanidine, the number of cells with foci was found to correlate exactly with the number of [PSI+ ] cells, regardless of the curing method. Therefore, the fluorescent foci are the prion seeds required for maintenance of [PSI+ ] and inactivation of Hsp104 cures [PSI+ ] by preventing severing of the prion seeds. During curing with guanidine, the reduction in seed size is an Hsp104-dependent effect that cannot be explained by limited severing of the seeds. Instead, in the presence of guanidine, Hsp104 retains an activity that trims or reduces the size of the prion seeds by releasing Sup35 molecules that are unable to form new prion seeds. This Hsp104 activity may also occur in propagating yeast.
Related Links	http://dx.doi.org/10.1371/journal.pone.0037692
Starting Page	37692
File Format	PDF
ISSN	19326203
e-ISSN	19326203
Journal	PLoS ONE
Issue Number	6
Volume Number	7
Language	English
Publisher	Public Library of Science
Publisher Date	2012-06-01
Access Restriction	Open
Rights Holder	Public Library of Science
Subject Keyword	Biochemistry, Genetics and Molecular Biology(all) Agricultural and Biological Sciences(all) Medicine(all) Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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The Schizosaccharomyces pombe Hsp104 Disaggregase Is Unable to Propagate the [PSI +] Prion

Regulation of the Hsp104 Middle Domain Activity Is Critical for Yeast Prion Propagation

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Heat shock protein 104 (Hsp104)-mediated curing of [PSI+] yeast prions depends on both [PSI+] conformation and the properties of the Hsp104 homologs

Hsp104-Dependent Remodeling of Prion Complexes Mediates Protein-Only Inheritance

Curing of yeast [PSI+] prion by guanidine inactivation of Hsp104 does not require cell division.

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