Fig. 2. The dimerization of CTD is required for DSAD1 binding.

a Close-up view of DSAD1 binding site on the C-terminal domain (CTD) of DSR2. The DSR2-A molecule is colored in the same scheme as in Fig. 1a, and the DSR2-B molecule is colored in gray for clarity. The DSAD1 protein is colored in orange. b Detailed insights into the interaction between DSAD1 and the H3 subdomain of DSR2. Key interacting residues are shown in stick representation. c Detailed insights into the interaction between DSAD1 protein and the H3 and H4 subdomains of DSR2 dimer. Key interacting residues are shown in stick representation. d In vitro pull-down of wild-type (WT) DSR2 and mutants by His-tagged DSAD1. ΔH4 indicates the deletion of H4 subdomain (aa 1–860). The K960A/D993A mutation had little impact on the DSR2-DSAD1 association. The gel represents three independent replicate experiments. Source data are provided as a Source data file.