Yeast Sup35 can misfold and form aggregates to create a prion phenotype, [PSI+]. The mechanisms through which two dominant-negative mutations in Sup35 (Q24R and G58D) cause prion curing are now investigated. The work reveals that the mutations affect the dynamics of aggregates in cells, leading to their resolubilization by the chaperone Hsp104.
- Susanne DiSalvo
- Aaron Derdowski
- Tricia R Serio
