The prion domain of yeast Ure2p induces autocatalytic formation of amyloid fibers by a recombinant fusion protein.

@article{Schlumpberger2000ThePD,
  title={The prion domain of yeast Ure2p induces autocatalytic formation of amyloid fibers by a recombinant fusion protein.},
  author={Martin Schlumpberger and Holger Wille and Michael R Baldwin and David A. Butler and Ira Herskowitz and Stanley B. Prusiner},
  journal={Protein science : a publication of the Protein Society},
  year={2000},
  volume={9 3},
  pages={
          440-51
        }
}
The Ure2 protein from Saccharomyces cerevisiae has been proposed to undergo a prion-like autocatalytic conformational change, which leads to inactivation of the protein, thereby generating the [URE3] phenotype. The first 65 amino acids, which are dispensable for the cellular function of Ure2p in nitrogen metabolism, are necessary and sufficient for [URE3] (Masison & Wickner, 1995), leading to designation of this domain as the Ure2 prion domain (UPD). We expressed both UPD and Ure2 as… CONTINUE READING
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