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High-throughput Screening for Protein-based Inheritance in S. cerevisiae
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The [URE3] prion in Candida.

Herman K Edskes1, Reed B Wickner

  • 1Laboratory of Biochemistry and Genetics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health, Bethesda, Maryland, USA.

Eukaryotic Cell
|February 12, 2013
PubMed
Summary
This summary is machine-generated.

The prion-forming ability of Ure2p protein is not conserved across species. Even in its native environment, Ure2p from Candida glabrata cannot form a prion, unlike Ure2p from Candida albicans.

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Area of Science:

  • Molecular biology
  • Protein biochemistry
  • Yeast genetics

Background:

  • Ure2p in Saccharomyces cerevisiae is a regulator of nitrogen catabolism and can form a prion, known as [URE3].
  • Previous studies demonstrated that Ure2p from Candida albicans (CaUre2p) can form a prion, but Ure2p from Candida glabrata (CgUre2p) cannot, even when tested in S. cerevisiae.

Purpose of the Study:

  • To investigate whether CgUre2p can form a prion within its native C. glabrata environment.
  • To determine if prion formation is an evolutionarily conserved trait of Ure2p or a sporadic occurrence.

Main Methods:

  • Construction of C. glabrata strains engineered to express either CaUre2p or CgUre2p.
  • Assaying prion formation of these Ure2p variants within the C. glabrata host.
  • Analysis of prion transmissibility and sequence homology of prion domains.

Main Results:

  • CaUre2p successfully formed a [URE3] prion in C. glabrata, while CgUre2p failed to form a prion, despite having a prion domain sequence more similar to S. cerevisiae Ure2p.
  • Certain variants of the [URE3albicans] prion exhibited restricted transmissibility to specific recipient C. glabrata strains.
  • The HO endonuclease in C. glabrata was shown to induce switching of the mating type locus.

Conclusions:

  • Prion formation by Ure2p is not a conserved biological property but rather a sporadic pathological event.
  • The ability of Ure2p to form prions is influenced by factors beyond prion domain sequence similarity.
  • Prion variants can display strain-specific transmissibility, and C. glabrata possesses mechanisms for mating type switching.