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. 2014 Jan 23;9(1):e87521. doi: 10.1371/journal.pone.0087521

Table 1. Summary of biochemical and biological effects of the Hsp104 M-domain mutants.

WT V426I V426C D434A K480C Y507D
ATPase Activity + + ++ ++
Hexamerization + + + +
Temp. Sensitivity + + + + ++ ++
Thermotolerance + + + +/− +/−
Luciferase Refolding + +/− +/− +/− +/−
Strong [ PSI +] 2n + +/− +/− +/− +/−
Weak [ PSI +] 2n + + +/− +/− +/−
Strong [ PSI +] n + +/− +/− +/− NT
Weak [ PSI +] n + +/− NT
s.d. low [ RNQ +] + + +/−
s.d. med [ RNQ +] +
s.d. high [ RNQ +] + + +/− +/−
s.d. very high [ RNQ +] + +
m.d. high [ RNQ +] + + +/− +/− +

Effects of Hsp104 mutations were characterized as follows for the indicated properties and prion propagation, as compared to wild type (WT) Hsp104: (+) comparable to WT, (+/−) some defect, (−) abolished/cured, or (++) enhanced activity or sensitivity. NT: not tested, 2n: yeast diploids, n: yeast haploids.