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. Author manuscript; available in PMC: 2022 Mar 1.
Published in final edited form as: Nature. 2021 Aug 18;597(7874):132–137. doi: 10.1038/s41586-021-03824-5

Fig. 3 |. Other polyD/E proteins can function as molecular chaperones, disaggregases, and unfoldases.

Fig. 3 |

a, The occurrence of each amino acid in DAXX-binding peptides relative to its occurrence in the peptide library (100%). b, Reactivation of denatured luciferase (50 nM) by DAXX and HSPs (100 nM) in the presence of increasing salt concentration. c, d, Activity (c) and solubility (d) of denatured luciferase (d-Luc; 5 nM) after incubation with DAXX, DAXX(ΔD/E), or DAXX(D/E). n-Luc, native luciferase. e, f, Heat-induced aggregation of luciferase (200 nM) in the absence or presence of GST, ANP32A (e) or SET (f). g, i, Prevention (g) and reversal (i) of ATXN1(82Q) (50 nM) aggregation by SET and ANP32A (200 nM each). h, j, Reactivation of heat-denatured luciferase (5 nM) (h) and misfolded LucD monomers (50 nM) (j) by SET and ANP32A (200 nM each). Data are mean or mean ± s.d. (n = 3) and are representative of three independent experiments.