A brief overview of the Swi1 prion—[SWI+]

Dustin K. Goncharoff, Zhiqiang Du, Liming Li

Research output: Contribution to journalReview articlepeer-review

8 Scopus citations


Prion and prion-like phenomena are involved in the pathology of numerous human neurodegenerative diseases. The budding yeast, Saccharomyces cerevisiae, has a number of endogenous yeast prions—epigenetic elements that are transmitted as altered protein conformations and often manifested as heritable phenotypic traits. One such yeast prion, [SWI+], was discovered and characterized by our laboratory. The protein determinant of [SWI+], Swi1 was found to contain an amino-terminal, asparagine-rich prion domain. Normally, Swi1 functions as part of the SWI/SNF chromatin remodeling complex, thus, acting as a global transcriptional regulator. Consequently, prionization of Swi1 leads to a variety of phenotypes including poor growth on non-glucose carbon sources and abolishment of multicellular features—with implications on characterization of [SWI+] as being detrimental or beneficial to yeast. The study of [SWI+] has revealed important knowledge regarding the chaperone systems supporting prion propagation as well as prion–prion interactions with [PSI+] and [RNQ+]. Additionally, an intricate regulatory network involving [SWI+] and other prion elements governing multicellular features in yeast has begun to be revealed. In this review, we discuss the current understanding of [SWI+] in addition to some possibilities for future study.

Original languageEnglish (US)
Article numberfoy061
JournalFEMS yeast research
Issue number6
StatePublished - Sep 1 2018


  • Chaperones
  • Multicellularity
  • Prion
  • Prion-interactions
  • [SWI+]

ASJC Scopus subject areas

  • Microbiology
  • Applied Microbiology and Biotechnology

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