Remodeling of protein aggregates by Hsp104.
Hsp104 is molecular chaperone in the AAA+ family of ATPases that specializes in the resolubilization and refolding of thermally denatured proteins in yeast. In addition to providing high levels of thermotolerance, Hsp104 plays a pivotal role in the propagation of yeast prions, self-replicating, amyloid-like aggregates that are inherited during mitosis and meiosis. In this review, the structure and function of Hsp104 is discussed, its functional interaction with other molecular chaperones, and a model for disaggregation and refolding is proposed.
Glover
John R
JR
Department of Biochemistry, University of Toronto, Toronto, Ontario, Canada. john.glover@utoronto.ca
Lum
Ronnie
R
D006360:Heat-Shock Proteins / Q000737:chemistry* / Q000502:physiology*; D008954:Models, Biological; D008958:Models, Molecular; D011328:Prions / Q000737:chemistry* / Q000378:metabolism; D011487:Protein Conformation; D017510:Protein Folding; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology
D006360:Heat-Shock Proteins; D011328:Prions; D029701:Saccharomyces cerevisiae Proteins; C070972:HsP104 protein, S cerevisiae