Fig. 6: LGMDD1 G/F domain mutants inhibit Sis1-WT induced ATPase activity of Ssa1. | Nature Communications

Fig. 6: LGMDD1 G/F domain mutants inhibit Sis1-WT induced ATPase activity of Ssa1.

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. 6

Stimulation of Ssa1 ATPase activity in the presence of Rnq1 seeds formed at 18 °C. Sis1-mutants (Sis1-F106L a, or Sis1-F115I b) (0–0.08 µM) were titrated with Sis1-WT (0.03 µM) in the presence of Ssa1 (1 µM) and ATP (1 mM). The fraction of ATP converted to ADP was determined at 30 min. Data represented as mean ± SEM, n = 3 biologically independent samples. For a, b; values of the increasing concentration of LGMDD1 mutants (0.01–0.08 µM) were compared with Sis1-WT (0.03 µM) alone. For a (top to bottom); *p < 0.049, **p < 0.001, ***p < 0.0008, ***p < 0.0001, ***p < 0.0003, ***p < 2.18e−05, ***p < 2.62e−06. For b (top to bottom); **p < 0.007, *p < 0.012, *p < 0.01, ***p < 0.0008, ***p < 0.0001, ***p < 6.4e−05, ***p < 2.11e−05. p-values are reported for unpaired, two-sided t-test. Source data are provided as a Source data file.

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