A bipolar personality of yeast prion proteins

Hiroshi Kurahashi, Keita Oishi, Yoshikazu Nakamura

Research output: Contribution to journalReview articlepeer-review

6 Citations (Scopus)

Abstract

Prions are infectious, self-propagating protein conformations. [PSI +], [RNQ+] and [URE3] are well characterized prions in Saccharomyces cerevisiae and represent the aggregated states of the translation termination factor Sup35, a functionally unknown protein Rnq1 and a regulator of nitrogen metabolism Ure2, respectively. Overproduction of Sup35 induces the de novo appearance of the [PSI+] prion in [RNQ+] or [URE3] strain, but not in non-prion strain. However, [RNQ+] and [URE3] prions themselves, as well as overexpression of a mutant Rnq1 protein, Rnq1Δ100 and Lsm4, hamper the maintenance of [PSI+]. These findings point to a bipolar activity of [RNQ+], [URE3], Rnq1Δ100 and Lsm4, and probably other yeast prion proteins as well, for the fate of [PSI+] prion. Possible mechanisms underlying the apparent bipolar activity of yeast prions will be discussed.

Original languageEnglish
Pages (from-to)305-310
Number of pages6
JournalPrion
Volume5
Issue number4
DOIs
Publication statusPublished - 2011 Oct

Keywords

  • Lsm4
  • New1
  • Pin
  • Yeast prion
  • [PSI]
  • [RNQ1Δ100]
  • [RNQ]
  • [URE3]

ASJC Scopus subject areas

  • Biochemistry
  • Cellular and Molecular Neuroscience
  • Cell Biology
  • Infectious Diseases

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