Saccharomyces cerevisiae contains several prion elements, which are epigenetically transmitted as self-perpetuating protein conformations. One such prion is [SWI⁺ ], whose protein determinant is Swi1, a subunit of the SWI/SNF chromatin-remodeling complex. We previously reported that [SWI⁺ ] formation results in a partial loss-of-function phenotype of poor growth in nonglucose medium and abolishment of multicellular features. We also showed that the first 38 amino acids of Swi1 propagated [SWI⁺]. We show here that a region as small as the first 32 amino acids of Swi1 (Swi1_1-32) can decorate [SWI⁺] aggregation and stably maintain and transmit [SWI⁺] independently of full-length Swi1. Regions smaller than Swi1_1-32 are either incapable of aggregation or unstably propagate [SWI⁺]. When fused to Sup35MC, the [PSI⁺ ] determinant lacking its PrD, Swi1_1-31 and Swi1_1-32 can act as transferable prion domains (PrDs). The resulting fusions give rise to a novel chimeric prion, [SPS⁺], exhibiting [PSI⁺]-like nonsense suppression. Thus, an NH₂-terminal region of ∼30 amino acids of Swi1 contains all the necessary information for in vivo prion formation, maintenance, and transmission. This PrD is unique in size and composition: glutamine free, asparagine rich, and the smallest defined to date. Our findings broaden our understanding of what features allow a protein region to serve as a PrD.

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Valtierra S, Du Z, Li L

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