title: Chaperone effects on prion and nonprion aggregates.
abstract: Exposure to high temperature or other stresses induces a synthesis of heat shock proteins. Many of these proteins are molecular chaperones, and some of them help cells to cope with heat-induced denaturation and aggregation of other proteins. In the last decade, chaperones have received increased attention in connection with their role in maintenance and propagation of the Saccharomyces cerevisiae prions, infectious or heritable agents transmitted at the protein level. Recent data suggest that functioning of the chaperones in reactivation of heat-damaged proteins and in propagation of prions is based on the same molecular mechanisms but may lead to different consequences depending on the type of aggregate. In both cases the concerted and balanced action of "chaperones' team," including Hsp104, Hsp70, Hsp40 and possibly other proteins, determines whether a misfolded protein is to be incorporated into an aggregate, rescued to the native state or targeted for degradation.
authors.affiliation: Siberian Institute of Plant Physiology and Biochemistry, Russian Academy of Sciences, Irkutsk, Russia.
authors.forename: Eugene G
authors.initials: EG
authors.lastname: Rikhvanov
authors.forename: Nina V
authors.initials: NV
authors.lastname: Romanova
authors.forename: Yury O
authors.initials: YO
authors.lastname: Chernoff
mesh_terms: D006360:Heat-Shock Proteins / Q000378:metabolism*; D006358:Hot Temperature; D011328:Prions / Q000378:metabolism*; D017510:Protein Folding; D012441:Saccharomyces cerevisiae / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000378:metabolism*
chemical_list: D006360:Heat-Shock Proteins; D011328:Prions; D029701:Saccharomyces cerevisiae Proteins