Fig. 2: Interfaces between SUV420H1(1–390) and the H4 tail together with DNA.
From: Structural basis of nucleosomal H4K20 recognition and methylation by SUV420H1 methyltransferase
a Overview of the recognition interfaces between SUV420H1(1–390) and nucleosomal H4 tail and DNA components. SUV420H1(1–390) domains are colored as shown in Fig. 1d. Histones H4 and DNA are colored in light green and orange, respectively. b Detailed view of the interactions between SUV420H1(1–390) and the phosphate backbone of nucleosome SHL 2 DNA. Important residues at the interface are shown as sticks. c Detailed view of the interactions between SUV420H1(1–390) and the H4 tail Q27. Important residues at the interface are shown as sticks. d Detailed view of the recognition interfaces between SUV420H1 and nucleosomal H4 tail. Residues at the interface of H4 are shown as sticks in green. H3 is colored in blue. SAM is colored in yellow. e Catalytic activity of wild-type SUV420H1(1–390) and various mutants on NCPH2A by end-point HMT assays in vitro. Adjusted P values for pairwise ANCOVA comparison of wild-type SUV420H1(1–390) and each mutant are reported: **** P < 0.0001. f MST binding assays of wild-type SUV420H1(1–390) and SUV420H1(1–390) mutants on NCPH2A. Error bars represent mean ± SEM based on 3 independent measurements. g Alignment of the apo SUV420H1 (Protein Data Bank (PDB) code 3S8P, grey) with SUV420H1(1–390)–NCPH2A complex (colored as in Fig. 1d). Directions of shifted regions of SUV420H1(1–390)–NCPH2A are indicated with black arrows. h Catalytic activity of SUV420H1(1–390) on NCPH2A and NCPH4Q27A by end-point HMT assays in vitro. ****P < 0.0001. i Detailed view of the interaction interface of SUV420H1 residue K258 in a negatively charged pocket. The important residues are shown as sticks.
