U.S. Department of Health and Human Services
Reed Wickner
 

 Contact Info

 
Tel: 301-496-3452
Email: wickner@helix.nih.gov
 

 Select Experience

 
  • M.D.Georgetown University1966
  • B.A.Cornell University1962
 

 Related Links

 

    Specialties
    • Biomedical Engineering/Biophysics/Physics
    • Genetics/Genomics
    • Microbiology/Infectious diseases (non-viral)
    • Molecular Biology/Biochemistry
    • Prions

    ​Research Images

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    TitleDescriptionImage
    Figure 1. Three genetic criteria for a yeast prion[URE3] is a non-Mendelian genetic element of S. cerevisiae that makes cells able to take up ureidosuccinate when ammonia is the nitrogen source.  [PSI] is a non-Mendelian genetic element that increases the efficiency with which weak suppressor tRNAs allow read-through of translation termination codons.  Three properties of these genetic elements indicated to us that they were prions of Ure2p and Sup35p, respectively: (1) reversible curability, (2) overproduction of the prion protein inducing prion formation de novo, and (3) similarity of prion phenotype and phenotype of mutation of the gene encoding the prion protein (with prion propagation depending on that gene).  These three properties allowed us to first identify these yeast non-chromosomal genetic elements as prions.Figure 1. Three genetic criteria for a yeast prionEnlarge
    Figure 2. Prion domains of yeast prion proteinsFor each of the yeast and fungal prions, a restricted portion of the protein is necessary and sufficient for generation and propagation of the prion.  These domains are generally rich in glutamine and asparagine and are the part of the protein that comprises the core of the amyloid in an in-register parallel structure.Figure 2. Prion domains of yeast prion proteinsEnlarge
    Figure 3. Model of yeast prion amyloid structureThe parallel in-register architecture of yeast prion amyloids features the favorable interaction between aligned identical amino acid side-chains.  This structure can explain how proteins can template their own conformation and how a protein can act as a gene.Figure 3. Model of yeast prion amyloid structureEnlarge