The glutamine- and asparagine-rich protein, Rnq1, is a putative yeast prion. Rnq1 protein with yet unknown function, can exists in either noninfectious soluble monomer form, [pin-], or the insoluble aggregated amyloid-like form called [PIN+]. The insoluble state is dominant and transmitted between cells through the cytoplasm. Rnq1 protein is necessary for the de novo induction of another prion, [PSI+]. The molecular chaperone Hsp104 is necessary for the aggregate formation of polyglutamine and for the maintenance of prion phenotype. The pre-existing aggregates are required for the chaperon-dependent establishment of the epigenetic trait in yeast prions.
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