Fig. 1: Cryo-EM structure of the DIM2-HP1 complex.
From: Multi-layered heterochromatin interaction as a switch for DIM2-mediated DNA methylation
a Domain architecture of DIM2 and HP1, with individual domains color coded and delimited by amino acid numbers. The DIM2 fragment used for structural and biochemical characterization is indicated by arrows. b In vitro DNA methylation assay of DIM2 on a (CTA)12/(TAG)12 36-mer DNA duplex, in the presence or absence of HP1 and/or histone peptides (H31-24K9me3 or H31-24K9me0). Data are mean ± s.d. (n = 3 biological replicates). The two-tailed Student’s t test statistical analysis was performed to compare DIM2 activity in the absence vs. presence of HP1 and/or histone peptides. ns not significant; ****p < 0.0001. Source data are provided as a Source Data file. c, d Two oppositive views of the cryo-EM density map of the DIM2-HP1 complex. e, f Atomic model of the DIM2-HP1 complex in two opposite views, with individual domains of DIM2 color coded. The two HP1 CSD subunits are colored in magenta. The NT and domain linkers are colored gray. The SAH molecule and zinc ion are shown in sphere representation. The color scheme for the individual domains of DIM2 is applied to subsequent figures unless otherwise indicated. g Cryo-EM density map for the SAH molecule bound to DIM2.
