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Prion-forming ability of Ure2 of yeasts is not evolutionarily conserved

Herman K Edskes1, Abbi Engel, Lindsay M McCann

  • 1National Institute of Diabetes, Digestive, and Kidney Diseases, National Institutes of Health, Bethesda, MD, USA.

Genetics
|March 4, 2011
PubMed

Insights

The prion [URE3] from yeast can infect other yeast species. Sequence conservation in Ure2p is not essential for prion formation, challenging previous assumptions about its function.

Area of Science:

  • Microbiology
  • Molecular Biology
  • Protein Science

Background:

  • The [URE3] prion is an infectious protein derived from Saccharomyces cerevisiae Ure2p, a key regulator of nitrogen catabolism.
  • Prions are self-propagating protein conformations that can alter cellular function.
  • The prion domain of Ure2p has conserved sequences across species, hypothesized to be crucial for prion formation and host benefit.

Purpose of the Study:

  • To investigate the infectivity of the [URE3] prion in wild Saccharomyces paradoxus.
  • To determine if Ure2p proteins from other yeast species, Candida albicans and Candida glabrata, can form the [URE3] prion.
  • To assess the role of conserved amino acid sequences in the prion domain of Ure2p for prion formation.

Main Methods:

  • Infection of wild S. paradoxus with the [URE3] prion.
  • Expression and functional analysis of Candida albicans and Candida glabrata Ure2p in S. cerevisiae.
  • Assessment of prion formation based on phenotypic changes in S. cerevisiae.

Main Results:

  • Wild S. paradoxus can be infected with the [URE3] prion, validating S. cerevisiae as a prion research model.
  • Ure2p from both C. albicans and C. glabrata were found to regulate nitrogen catabolism.
  • C. albicans Ure2p, lacking conserved prion domain sequence, formed the [URE3] prion in S. cerevisiae.
  • C. glabrata Ure2p, possessing the conserved sequence, failed to form the [URE3] prion in S. cerevisiae.

Conclusions:

  • The [URE3] prion can infect different yeast species, expanding the scope of prion research.
  • Sequence conservation within the Ure2p prion domain is not a prerequisite for [URE3] prion formation.
  • The findings challenge the hypothesis that sequence conservation is solely for maintaining prion-forming ability, suggesting alternative evolutionary pressures.

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