Article
N-terminal domain of yeast Hsp104 chaperone is dispensable for thermotolerance and prion propagation but necessary for curing prions by Hsp104 overexpression.
Genetics - 1 Jun 2006
Hung Guo-Chiuan, Masison Daniel C
Abstract excerpt
Hsp104 is a hexameric protein chaperone that resolubilizes stress-damaged proteins from aggregates. Hsp104 promotes [PSI(+)] prion propagation by breaking prion aggregates, which propagate as amyloid fibers, into more numerous prion "seeds." Inactivating Hsp104 cures cells of [PSI(+)] and other amyloid-like yeast prions. Overexpressing Hsp104 also eliminates [PSI(+)], presumably by completely resolubilizing prion...
Topics
- Alleles
- Gene Expression
- Genes, Fungal
- HSP70 Heat-Shock Proteins
- Heat-Shock Proteins
- Luciferases
- Mutagenesis
- Peptide Termination Factors
- Prions
- Protein Structure, Quaternary
- Protein Structure, Tertiary
- Saccharomyces cerevisiae
- Saccharomyces cerevisiae Proteins
- Temperature