Abstract
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 language | English (US) |
---|---|
Article number | foy061 |
Journal | FEMS yeast research |
Volume | 18 |
Issue number | 6 |
DOIs | |
State | Published - Sep 1 2018 |
Funding
This work is supported by a grant from the U.S. National Institutes of Health (R01GM110045) to LL.
Keywords
- Chaperones
- Multicellularity
- Prion
- Prion-interactions
- SWI/SNF
- [SWI+]
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology
- Microbiology