Extended Data Fig. 9. Similarity of the ARDs in TONSL and BARD1, and protein inputs.

a, Superposition of the structures of TONSL ARD and BARD1 ARD (PDB 3C5R, Fox D. 3rd et al. JBC 2008). The main residues involved in TONSL ARD interactions with the H4 tail are compared to the corresponding residues of BARD1 ARD. The two ARDs show highly similar topology and conservation of the histone-binding surface. b, Input material of the experiment in Fig. 1h. c, Input material of the experiment in Fig. 1j. d, Spot assay with biotinylated H4 tail (aa. 14-33) peptides confirming equal input into pull down reactions. e, Input material of the experiment in Fig. 4b. f, Input material of the NCC experiment in Fig. 4c. Note that because ARD mutation disrupts chromatin binding in the presence and absence of CPT (Fig. 3e-f, 4a), GFP-TONSL N517 levels are low in the input chromatin. The NCC experiment in Fig. 4c supports our microscopy-based data (Fig. 4a) and further shows that there is no local accumulation of the GFP-TONSL ARD mutant at damaged forks that could have been missed in our microscopy-based quantification of total TONSL on chromatin.