Prions are proteins that can exist under the same conditions in two or more conformations, and at least one of them has infectious properties. Typically, acquisition of such infectious prion conformation is associated with the formation of amyloids, i.e., protein aggregates with a characteristic spatial structure. To date, about 10 prions have been identified in yeast Saccharomyces cerevisiae. One of the key regulators of nitrogen metabolism in S. cerevisiae, Gln3, contains amyloidogenic region manifesting prion-like properties. Prion properties of the full-length Gln3 have not been analyzed before. In this study, we demonstrated that amyloidogenic region of Gln3 is able to act as a template initiating aggregation of the overproduced full-length Gln3 protein in the presence of the [PIN⁺] prion. The aggregated state of the full-length Gln3 has prion-like properties, including infectivity and curability by anti-prion agent guanidine hydrochloride, but propagates only when overpro