Fig. 3: Contacts with H2A–H2B acidic patch by SUV420H1(1–390) CTD domain orient SUV420H1 onto nucleosome.
From: Structural basis of nucleosomal H4K20 recognition and methylation by SUV420H1 methyltransferase
a Overview of the contacts between SUV420H1(1–390) CTD domain and nucleosomal H2A–H2B acidic patch. SUV420H1(1–390) are colored the same as Fig. 1d. Histones H2A and H2B are colored in yellow and pink, respectively. b, c, f Detailed view of the recognition of the acidic patch of the nucleosome by arginine anchors. Important residues at the interface are shown as sticks. d MST binding assays of wild-type SUV420H1(1–390) and SUV420H1(1–390) mutants with NCPH4K20M. Error bars represent mean ± SEM based on three independent measurements. e Catalytic activity of wild-type SUV420H1(1–390) and various mutants on NCPH2A by end-point HMT assays in vitro. Each assay was repeated at least three times with similar results. ****P < 0.0001. g Sequence alignment of the region containing D97 and S98 of H2A.Z and the corresponding region of H2A (in single-letter code). The same residues are boxed in a purple background. h Conformational changes and shifts of residue 220 in SUV420H1(1–390)–NCPH2A and SUV420H1(1–390)–NCPH2A.Z complexes. Directions of shifted regions are indicated with black arrows. i Catalytic activity of SUV420H1(1–390) on NCPH2A, NCPH2A.Z and NCPH2A.Z(D97N/S98K) by end-point HMT assays in vitro. The catalytic activity of SUV420H1(1–390) R220A on NCPH2A and NCPH2A.Z by end-point HMT assays in vitro. Each assay was repeated at least three times with similar results. ***P = 0.0006, **P = 0.0086. j MST binding assays of wild-type SUV420H1(1–390) on NCPH2A, NCPH2A.Z, NCPH2A.Z(D97N/S98K) containing H4K20.
