Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities.

@article{Shorter2006DestructionOP,
  title={Destruction or potentiation of different prions catalyzed by similar Hsp104 remodeling activities.},
  author={James Shorter and Susan Lindquist},
  journal={Molecular cell},
  year={2006},
  volume={23 3},
  pages={425-38}
}
Yeast prions are protein-based genetic elements that self-perpetuate changes in protein conformation and function. A protein-remodeling factor, Hsp104, controls the inheritance of several yeast prions, including those formed by Sup35 and Ure2. Perplexingly, deletion of Hsp104 eliminates Sup35 and Ure2 prions, whereas overexpression of Hsp104 purges cells of Sup35 prions, but not Ure2 prions. Here, we used pure components to dissect how Hsp104 regulates prion formation, growth, and division. For… CONTINUE READING

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