Table 2.

Examples of yeast and fungal amyloid-based prions.

Species and protein	Cellular function	QN-rich PrD(s)	Prion designation
Saccharomyces cerevisiae
Sup35 (eRF3)	Translation termination (release) factor	Yes	[PSI+]a
Ure2	Regulatory protein in nitrogen metabolism	Yes	[URE3]b
Rnq1	Unknown	Yes	[RNQ+] or [PIN+]c
Swi1	Chromatin remodeling factor	Yes	[SWI+]d
Cyc8	Transcriptional corepressor	Yes	[OCT+]e
Mot3	Transcriptional repressor	Yes	[MOT3+]f
Nup100	FG-nucleoporin	Yes	[NUP100+]g
Lsb2	Stress-inducible cytoskeletal protein	Yes	[LSB+]h
Mod5	tRNA isopentenyltransferase	No	[MOD+]i
Podospora anserina
Het-s	Cytoplasmic incompatibility	No	[HetS]j

^aCox (1965) and Wickner (1994).

^bLacroute (1971) and Wickner (1994).

^cThe term [PIN⁺], from “[PSI⁺] inducibility” has initially been introduced to designate the specific prion factor that promoted de novo formation of [PSI⁺] (Derkatch, Bradley, Zhou, Chernoff, & Liebman, 1997) and has later been identified as a prion form of Rnq1 protein (Derkatch, Bradley, Hong, & Liebman, 2001). Rnq1 prion was termed [RNQ⁺] in an independent paper (Sondheimer, Lopez, Craig, & Lindquist, 2001). Other prions may also exhibit Pin⁺ phenotype.

^dDu, Park, Yu, Fan, and Li (2008).

^ePatel, Gavin-Smyth, and Liebman (2009).

^fAlberti, Halfmann, King, Kapila, and Lindquist (2009) and Holmes, Lancaster, Lindquist, and Halfmann (2013).

^gHalfmann, Wright, Alberti, Lindquist, and Rexach (2012).

^hChernova, Kiktev, et al. (2017).

ⁱSuzuki, Shimazu, and Tanaka (2012).

^jCoustou, Deleu, Saupe, and Begueret (1997) and Maddelein, Dos Reis, Duvezin-Caubet, Coulary-Salin, and Saupe (2002).