A regulatory role of the Rnq1 nonprion domain for prion propagation and polyglutamine aggregates

Hiroshi Kurahashi, Masao Ishiwata, Shoichiro Shibata, Yoshikazu Nakamura

Research output: Contribution to journalArticlepeer-review

24 Citations (Scopus)

Abstract

Prions are infectious, self-propagating protein conformations. Rnq1 is required for the yeast Saccharomyces cerevisiae prion [PIN+], which is necessary for the de novo induction of a second prion, [PSI+]. Here we isolated a [PSI+]-eliminating mutant, Rnq1Δ100, that deletes the nonprion domain of Rnq1. Rnq1Δ100 inhibits not only [PSI +] prion propagation but also [URE3] prion and huntingtin's polyglutamine aggregate propagation in a [PIN+] background but not in a [pin-] background. Rnq1Δ100, however, does not eliminate [PIN+]. These findings are interpreted as showing a possible involvement of the Rnq1 prion in the maintenance of heterologous prions and polyQ aggregates. Rnq1 and Rnq1Δ100 form a sodium dodecyl sulfate-stable and Sis1 (an Hsp40 chaperone protein)-containing coaggregate in [PIN +] cells. Importantly, Rnq1Δ100 is highly QN-rich and prone to self-aggregate or coaggregate with Rnq1 when coexpressed in [pin-] cells. However, the [pin-] Rnq1-Rnq1Δ100 coaggregate does not represent a prion-like aggregate. These findings suggest that [PIN+] Rnq1-Rnq1Δ100 aggregates interact with other transmissible and nontransmissible amyloids to destabilize them and that the nonprion domain of Rnq1 plays a crucial role in self-regulation of the highly reactive QN-rich prion domain of Rnq1.

Original languageEnglish
Pages (from-to)3313-3323
Number of pages11
JournalMolecular and cellular biology
Volume28
Issue number10
DOIs
Publication statusPublished - 2008 May

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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