EdskesTOF2Supple.zip (2.48 MB)
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Supplemental Material for Edskes, et al., 2021

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posted on 04.03.2021, 18:43 by Herman K. Edskes, Emily E. Stroobant, Morgan P. DeWilde, Evgeny E. Bezsonov, Reed B. Wickner
The Supplementary Information includes extended SILAC methods, strains of S. cerevisiae (Table S1), primers used (Table S2), proteins increased 1.5-fold or more in abundance in pre9Δ (Table S3), Proteins decreased 1.5-fold or more in abundance in pre9Δ (Table S4), a diagram of the proteasome α ring (Fig. S1), evidence that proteasome – related knockouts do not affect [PSI+] propagation (Fig. S2), evidence that [URE3-1] is less stable in 779-6A pre9Δ than in BY241 pre9Δ (Fig. S3), data showing that levels of Sup35p are not affected by proteasome – related mutations in strain BY241 (Fig. S4), data showing Btn2p levels in proteasome mutants are elevated by the presence of [PSI+] (Fig. S5 and S6), measuring the absolute levels of Btn2p and Cur1p in strain 779-6A by comparison with purified recombinant Btn2-His6 and Cur1-His6 (Fig. S7), the multiple bands of Cur1p (Fig. S8), the elevation of Btn2p in tof2 mutants (Fig. S9) and the absence of a ubiquitin ladder of Btn2p in a pre9Δ strain (Fig. S10). Table S5 compares protein turnover rates with their levels by SILAC in pre9Δ strains.


Article title

Proteasome control of [URE3] prion propagation by degradation of anti-prion proteins Cur1 and Btn2 in Saccharomyces cerevisiae

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