Extended Data Figure 4. Structural comparison of the ARDs of TONSL and GLP.

a, b, Representative view of the TONSL ARD with histone H4 tail (a, this work), and crystal structure of the GLP ARD in complex with histone H3 tail dimethylated at Lys9 (Collins R.E. et al. NSMB 2008) (b). Both TONSL ARD and GLP ARD use the concave surface to bind their cognate target H4 tail and H3 tail, respectively. TONSL ARD recognizes H4K20me0 mainly through 3 strong hydrogen bonds with acidic residues Glu530, Asp559 and Glu568, while GLP ARD recognizes H3K9me2 mainly through an aromatic cage forming by residues Trp839, Trp844, Glu847 and Trp877. c, ITC analysis of TONSL ARD binding to H3K9me1 peptide. d, ITC analysis of TONSL acidic stretch and ARD (a.a. 450-692) with H3K9me1 (a.a. 1-21) and H4 (a.a. 9-25) peptides.