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Prion domains: sequences, structures and interactions

Eric D Ross1, Allen Minton, Reed B Wickner

  • 1Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland 20892-0830, USA. wickner@helix.nih.gov

Nature Cell Biology
|December 31, 2005
PubMed

Insights

Prions are infectious proteins forming amyloid structures. Specific prion domains drive this self-propagation, and their structure is key to prion formation in yeast proteins like Ure2p and Sup35p.

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Prions are infectious proteins characterized by self-propagating amyloid structures.
  • The prion domain (PD) is crucial for amyloid core formation and infectivity.
  • Understanding PDs is key to deciphering prion propagation mechanisms.

Purpose of the Study:

  • To compare properties of known prion domains.
  • To investigate interactions between prion domains, full proteins, and chaperones.
  • To elucidate the structural basis of prion infectivity.

Main Methods:

  • Comparative analysis of known prion domains.
  • Biochemical assays to study protein interactions.
  • Structural studies to determine amyloid conformation.

Main Results:

  • Prion domains dictate infectious properties by forming the amyloid core.
  • Shuffling prion domains between yeast proteins Ure2p and Sup35p retains prion formation.
  • This suggests a conserved parallel in-register beta-sheet structure is fundamental.

Conclusions:

  • The prion domain's structure is the primary determinant of prion infectivity.
  • Conserved structural features of prion domains facilitate self-propagation.
  • Further research into prion domain structure can inform therapeutic strategies.

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