Reference: Kurahashi H, et al. (2008) A regulatory role of the Rnq1 nonprion domain for prion propagation and polyglutamine aggregates. Mol Cell Biol 28(10):3313-23

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Abstract


Prions are infectious, self-propagating protein conformations. Rnq1 is required for the yeast prion [PIN(+)], which is necessary for the de novo induction of a second prion, [PSI(+)]. Here we isolate a [PSI(+)]-eliminating mutant, Rnq1Delta100, that deletes the non-prion domain of Rnq1. Rnq1Delta100 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. Rnq1Delta100, however, does not eliminate [PIN(+)]. These findings are interpreted as showing a possible involvement of Rnq1 prion in the maintenance of heterologous prions and polyQ aggregates. Rnq1 and Rnq1Delta100 form a SDS-stable and Sis1 (a Hsp40 chaperone protein)-containing co-aggregate in [PIN(+)] cells. Importantly, Rnq1Delta100 is highly QN-rich and prone to self-aggregate or co-aggregate with Rnq1 when co-expressed in [pin(-)] cells. However, the [pin(-)] Rnq1-Rnq1Delta100 co-aggregate does not represent a prion-like aggregate. These findings suggest that [PIN(+)] Rnq1-Rnq1Delta100 aggregates interact with other transmissible and non-transmissible amyloids to destabilize them, and that the non-prion domain of Rnq1 plays a crucial role to self-regulate the highly reactive QN-rich prion domain of Rnq1.

Reference Type
Journal Article
Authors
Kurahashi H, Ishiwata M, Shibata S, Nakamura Y
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