Structure of the chromatin remodelling enzyme Chd1 bound to a ubiquitinylated nucleosome

Ramasubramanian Sundaramoorthy; Amanda L. Hughes; Hassane El-Mkami; David Norman; Tom Owen-Hughes

The structure of Chd1 nucleosome complexes As Chd1 functions on transcribed genes, it is of interest to understand the interplay between Chd1 and histone modifications observed in coding region chromatin. As a result nucleosomes were prepared in which histone H3 K36 was alkylated to mimic trimethylation ( The overall organisation of Chd1 is similar to that observed previously by cryo EM (Farnung et al., 2017; Sundaramoorthy et al., 2017) and directed crosslinking (Nodelman et al., 2017) . The ATPase domains are bound at the SHL-2 location. Of the two SHL2 locations within nucleosomes, the bound site is in closest proximity to SANT-SLIDE domain bound linker DNA in physical space, but distal on the unwrapped linear DNA sequence (Figure 1 ). Chd1 predominantly contacts the nucleosome via contacts with DNA, via the DNABD in the linker and ATPase lobes at SHL2, contacts with histones are limited to the histone H3 and H4 N-terminal regions discussed below.