Blessings in disguise: biological benefits of prion-like mechanisms

Trends Cell Biol. 2013 Jun;23(6):251-9. doi: 10.1016/j.tcb.2013.01.007. Epub 2013 Feb 26.


Prions and amyloids are often associated with disease, but related mechanisms provide beneficial functions in nature. Prion-like mechanisms (PriLiMs) are found from bacteria to humans, where they alter the biological and physical properties of prion-like proteins. We have proposed that prions can serve as heritable bet-hedging devices for diversifying microbial phenotypes. Other, more dynamic proteinaceous complexes may be governed by similar self-templating conformational switches. Additional PriLiMs continue to be identified and many share features of self-templating protein structure (including amyloids) and dependence on chaperone proteins. Here, we discuss several PriLiMs and their functions, intending to spur discussion and collaboration on the subject of beneficial prion-like behaviors.

MeSH terms

  • Amyloid / chemistry
  • Amyloid / genetics
  • Amyloid / metabolism*
  • Animals
  • Humans
  • Models, Biological
  • Peptide Termination Factors / genetics
  • Peptide Termination Factors / metabolism*
  • Prions / chemistry
  • Prions / genetics
  • Prions / metabolism*
  • Protein Conformation
  • Saccharomyces cerevisiae / metabolism
  • Saccharomyces cerevisiae Proteins / metabolism*
  • Signal Transduction


  • Amyloid
  • Peptide Termination Factors
  • Prions
  • Saccharomyces cerevisiae Proteins