Extended Data Fig. 1: Biochemical and structural characterizations of human MLL1–ubNCP complex. | Nature

Extended Data Fig. 1: Biochemical and structural characterizations of human MLL1–ubNCP complex.

From: Structural basis of nucleosome recognition and modification by MLL methyltransferases

Extended Data Fig. 1

a, Gel filtration (left) and SDS–PAGE analysis (right) of the assembly of the recombinant MLL1 complex, composed of full-length WRAD proteins and MLL1 (residues 3754–3969). Experiments were repeated at least three times with similar results. b, EMSAs of the recombinant human MLL1 complex with either unmodified or H2BK120ub1 NCPs at molar ratios of 1:1, 2:1 and 4:1. Top, input of the EMSA mixtures. Bottom, native PAGE analysis of the gel shifting of NCP and ubNCP by the MLL1 complex. Each assay was repeated at least three times with similar results. c, Flow chart of cryo-EM data processing of the MLL1–ubNCP dataset (resolution of 3.2 Å). Masked 3D classifications without realignment were applied to MLL1–WDR5 (left branch), ASH2L (middle branch) and RBBP5–ubiquitin (right branch).

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