Fig. 4: Structural and biochemical comparison between human SETD2–hNCPH3.3K36M and yeast Set2–xNCPH3K36M complexes. | Cell Discovery

Fig. 4: Structural and biochemical comparison between human SETD2–hNCPH3.3K36M and yeast Set2–xNCPH3K36M complexes.

From: Cryo-EM structure of SETD2/Set2 methyltransferase bound to a nucleosome containing oncohistone mutations

Fig. 4

a Schematic drawing of the domain organizations of yeast Set2. The color scheme is the same as that of the Set2–xNCPH3K36M structural model. b Cryo-EM density map and atomic model of yeast Set2–xNCPH3K36M complex shown from two orthogonal views. The cryo-EM map was segmented and colored according to the respective components of the Set2–xNCPH3K36M complex. c The detailed view of the active site in yeast Set2 and human SETD2. d HMT assays of wild-type and mutant Set2 (top) and SETD2 (bottom) proteins against nucleosome substrates. Mono-, di-, and tri-methylation levels of histone H3K36 are determined with antibodies of H3K36me1, H3K36me2, and H3K36me3. The input of the reactions is shown in Supplementary Fig. S10d. Each assay was repeated at least three times with similar results. e EMSAs of different truncations of Set2 (left) and SETD2 (right) with nucleosome at molar ratios of 1:1, 2:1, 4:1, and 8:1. The Native-PAGE gel is stained with ethidium bromide (EB) to show the gel shifting of NCP by Set2/SETD2. The input of the assays is shown in Supplementary Fig. S11d.

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