Fig. 5: LGMDD1 G/F domain mutants showed reduced dimerization. | Nature Communications

Fig. 5: LGMDD1 G/F domain mutants showed reduced dimerization.

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. 5

a For homodimerization, uncleaved His-tagged Sis1-WT and mutants (20 nM) were added into non-His-tagged (cleaved) Sis1-WT and mutants (200 nM) and adsorbed in microtiter plate wells. b For heterodimerization, uncleaved His-tagged Sis1-WT (20 nM) was added to cleaved mutants (200 nM) and adsorbed in microtiter plate wells. In both a, b, following adsorption, ELISA was performed using an anti-His antibody. Values shown are mean + SEM, n = 3 biologically independent samples. For a, b; all LGMDD1 mutants were compared with Sis1-WT; for F106L (***p < 0.0008 and **p < 0.003), for N108L (**p < 0.008 and **p < 0.004), for D110∆ (***p < 0.0006 and **p < 0.005), and for F115I (***p < 0.0009 and **p < 0.006) values are reported for unpaired, two-sided t-test. Source data are provided as a Source data file.

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