Prions, Chaperones, and Proteostasis in Yeast.
Prions are alternatively folded, self-perpetuating protein isoforms involved in a variety of biological and pathological processes. Yeast prions are protein-based heritable elements that serve as an excellent experimental system for studying prion biology. The propagation of yeast prions is controlled by the same Hsp104/70/40 chaperone machinery that is involved in the protection of yeast cells against proteotoxic stress. Ribosome-associated chaperones, proteolytic pathways, cellular quality-control compartments, and cytoskeletal networks influence prion formation, maintenance, and toxicity. Environmental stresses lead to asymmetric prion distribution in cell divisions. Chaperones and cytoskeletal proteins mediate this effect. Overall, this is an intimate relationship with the protein quality-control machinery of the cell, which enables prions to be maintained and reproduced. The presence of many of these same mechanisms in higher eukaryotes has implications for the diagnosis and treatment of mammalian amyloid diseases.
Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Tatiana A
TA
Chernova
Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
Keith D
KD
Wilkinson
School of Biological Sciences, Georgia Institute of Technology, Atlanta, Georgia 30332-2000.|Laboratory of Amyloid Biology and Institute of Translational Biomedicine, St. Petersburg State University, St. Petersburg 199034, Russia.
Yury O
YO
Chernoff
D006360:Heat-Shock Proteins / Q000378:metabolism; D018832:Molecular Chaperones / Q000378:metabolism*; D011328:Prions; D015003:Yeasts / Q000378:metabolism*
D006360:Heat-Shock Proteins; D018832:Molecular Chaperones; D011328:Prions