Table 4.

De novo [PSI⁺] nucleation by wild-type and altered derivatives of Aβ and PrP in yeast.^a

Protein	Derivative	Effect in vitro or in mammals/humans	Effect in yeast when fused to Sup35 PrD
PrP	90–230	Susceptible to TSE	Prion nucleation
	23–230	Susceptible to TSE, prone to instability	Increased prion nucleation
	120–230	Not susceptible to TSE	No prion nucleation
	90–144	Heritable TSE-like diseaseb	Increased prion nucleation
	90–159	Heritable TSE-like diseaseb	Increased prion nucleation
	90–171	Not testedc	Increased prion nucleation
	90–230 P101L	Heritable TSE	Increased prion nucleation
	90–230 Q167R	Inhibition of PrPSc propagation	Decreased prion nucleation
Aβ	1–42	High aggregation propensity	Prion nucleation
	1–40	Low aggregation propensity	Low prion nucleation
	1–42 19S, F20S,I31P	No amyloid formationd	No prion nucleation
	1–42 D23N	Heritable AD	Increased prion nucleation
	1–42 K28E	Aβ structure impairment?	Decreased prion nucleation

^aYeast data are from Chandramowlishwaran et al. (2018). See text for mammalian and in vitro references.

^bEffects of truncations in mammalian/human systems were studied within the context of a protein containing the full-length N-proximal region.

^cWhile this particular truncation has not been studied in mammals, it has been reported (after publication of yeast data) that a truncation at the aa position 169 of human PrP is associated with a TSE-like disease (Capellari et al., 2018).

^dIndividual substitutions were also tested in yeast, with a strongest effect detected for I31P.