Fig. 3: Stimulation of ATPase activity of Ssa1 by LGMDD1 G/F domain mutants is client-conformation specific. | Nature Communications

Fig. 3: Stimulation of ATPase activity of Ssa1 by LGMDD1 G/F domain mutants is client-conformation specific.

From: Disease-associated mutations within the yeast DNAJB6 homolog Sis1 slow conformer-specific substrate processing and can be corrected by the modulation of nucleotide exchange factors

Fig. 3

Stimulation of Ssa1 ATPase activity in the presence of Rnq1 seeds formed at a 18 °C, b 25 °C, and c 37 °C. Ssa1 (1 µM) in complex with ATP (1 mM) in the presence of Sis1-WT (black) or Sis1-mutants (Sis1-F106L (yellow), Sis1-N108L (red), Sis1-D110Δ (green), or Sis1-F115I (blue)) (0.05 µM). The fraction of ATP converted to ADP was determined. For a–c, a total of 10% seeds were used in a reaction. In all cases, only Ssa1 with Rnq1 (orange), Sis1 with Ssa1 (dark purple) and were used as controls. For a–c, Sis1-WT was compared with LGMDD1- mutants. Data are presented as mean values + SEM, n = 4 biologically independent samples. For a (left to right); ***p < 1.29e−07, ***p < 6.29e−08, ***p < 4.78e−07, ***p < 2.41e−07; for b (left to right); ***p < 4.64e−05, ***p < 6.31e−05, ***p < 0.0001, ***p < 0.0001; and for c (left to right); **p < 0.004, ***p < 2.63e−05, **p < 0.002, ***p < 9.59e−05. p-values are reported for unpaired, two-sided t-test. Source data are provided as a Source data file.

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