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Stress and prions: Lessons from the yeast model
Author(s) -
Chernoff Yury O.
Publication year - 2007
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2007.04.075
Subject(s) - yeast , chaperone (clinical) , protein aggregation , fungal prion , microbiology and biotechnology , chemistry , prion proteins , hsp70 , prion protein , amyloid (mycology) , protein folding , saccharomyces cerevisiae , biophysics , heat shock protein , biology , biochemistry , gene , medicine , inorganic chemistry , disease , pathology
Yeast self‐perpetuating amyloids (prions) provide a convenient model for studying the cellular control of highly ordered aggregates involved in mammalian protein assembly disorders. The very ability of an amyloid to propagate a prion state in yeast is determined by its interactions with the stress‐inducible chaperone Hsp104. Prion formation and propagation are also influenced by other stress‐related chaperones (Hsp70 and Hsp40), and by alterations of the protein trafficking and degradation networks. Some stress conditions induce prion formation or loss. It is proposed that prions arise as byproducts of the reversible assembly of highly ordered complexes, protecting certain proteins during unfavorable conditions.