Hsp70 Binding to the N-terminal Domain of Hsp104 Regulates [<i>PSI<sup>+</sup></i>] Curing by Hsp104 Overexpression-Reference-Cited by-同舟云学术

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Hsp70 Binding to the N-terminal Domain of Hsp104 Regulates [PSI⁺] Curing by Hsp104 Overexpression

Published:2023-04-03 Issue:4 Volume:43 Page:157-173
ISSN:1098-5549
Container-title:Molecular and Cellular Biology
language:en
Short-container-title:Molecular and Cellular Biology

Author:

Zhao Xiaohong¹,Stanford Katherine¹,Ahearn Joseph¹,Masison Daniel C.²,Greene Lois E.¹

Affiliation:

1. Laboratory of Cell Biology, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland, USA

2. Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA

Publisher

Informa UK Limited

Subject

Cell Biology,Molecular Biology

Link

https://www.tandfonline.com/doi/pdf/10.1080/10985549.2023.2198181

Reference48 articles.

1. [URE3] as an Altered URE2 Protein: Evidence for a Prion Analog in Saccharomyces cerevisiae

2. Protein inheritance (prions) based on parallel in-register β-sheet amyloid structures

3. The elimination of the yeast [PSI+] prion by guanidine hydrochloride is the result of Hsp104 inactivation

4. The Prion Curing Agent Guanidinium Chloride Specifically Inhibits ATP Hydrolysis by Hsp104

5. Amino acid residue 184 of yeast Hsp104 chaperone is critical for prion-curing by guanidine, prion propagation, and thermotolerance

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