Skip to main content
. Author manuscript; available in PMC: 2026 Jun 16.
Published in final edited form as: Mol Cell. 2026 Feb 24;86(5):834–850.e9. doi: 10.1016/j.molcel.2026.01.030

Figure 5: The PWWP domain scans the modification state of H3K36.

Figure 5:

a, b Cryo-EM maps of DNMT3A2/3B3 in complex with the unmodified (a) and H3K36me2 modified (b) 10-8-10 di-nucleosomes. Close-up views of each PWWP domain docked into the semi-transparent EM density are shown in the insets. H3 tail density connecting the PWWP domains to the nucleosome is outlined in black. c Composite Cryo-EM map of DNMT3A2/3B3 in complex with a H3K36me2 nucleosome with 10bp overhangs. Close-up views of each PWWP domain docked into the semi-transparent EM density are shown in the insets. d 10Å low pass filtered Cryo-EM map of DNMT3A2/3B3 bound to an unmodified nucleosome (gray, EMD-20281) superimposed with the composite Cryo-EM map of DNMT3A2/3B3 bound to a nucleosome modified with H3K36me2 (colored). Movements of DNMT3A2/3B3 that are triggered by PWWP binding to H3K36me2 are indicated using black arrows. e Working model for DNMT3A2/3B3 methylation on DNA linkers. See also Figure S6–S7.