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. Author manuscript; available in PMC: 2023 Nov 1.
Published in final edited form as: Nat Chem Biol. 2023 Feb 16;19(5):624–632. doi: 10.1038/s41589-023-01256-y

Fig. 4 |. Dynamic and multivalent KDM2A-nucleosome interactions.

Fig. 4 |

a, Basic histone surface exposed by DNA unwrapping between JmjC domain and acidic patch-binding region of KDM2A. b, Demethylation of H3K36me2-nucleosomes by WT and neutralized 23–33 mutant KDM2A. Relative residual H3K36me2 plotted as individual data points (n=6 assay technical replicates) along with mean ± SD, **p ≤0.01 (0.0014) using an unpaired two-tailed t-test. c-d, 3D classification in RELION (c) and heterogeneity analysis with cryoDRGN kmeans sampling (d) reveals correlated heterogeneity in regions of structure corresponding to JmjC domain and unwrapped DNA. e, Model of KDM2A-nucleosome binding includes dynamic and multivalent interactions with multiple nucleosome surfaces.