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Significance The [PSI+] prion (infectious protein) is an amyloid (filamentous polymer) of the Sup35 protein, producing detrimental effects on yeast. We find that at their normal expression levels the core components of nonsense-mediated mRNA decay for mRNA quality control, Upf1p, Upf2p, and Upf3p, block the propagation of most new [PSI+] prion variants. The curing mechanism relies upon both Sup35p-binding by each Upf protein and by the trimeric Upf complex. Our results support the notion that normal protein–protein interactions prevent abnormal interactions.

Nonsense-mediated mRNA decay factors cure most [PSI+] prion variants