Fig. 2: Interactions in the human SETD2–hNCPH3.3K36M complex. | Cell Discovery

Fig. 2: Interactions in the human SETD2–hNCPH3.3K36M complex.

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

Fig. 2

a Nucleosome DNA at SHL-6 and SHL-7 is detached from the core histones in the SETD2–hNCPH3.3K36M complex structure. b Detailed view of the recognition interface between SETD2AWS and the α-N helix of histone H3.3. c Endpoint HMT assays carried out with wide-type or mutant hNCP, revealing that mutations of Arg49H3.3 and Arg52H3.3 to Glu drastically diminished the enzymatic activities of SETD2 towards hNCP. The HMT activities were reported for equal amounts of the SETD2 proteins. Error bars correspond to the SD of three replicate assays. Input of the HMT reactions is shown in Supplementary Fig. S4a. d Endpoint HMT assays carried out with wide-type or mutant hNCP, revealing that mutation of Arg49H3.3 and Arg52H3.3 to Glu severely impaired the enzymatic activities of NSD1 towards hNCP. The HMT activities were reported for equal amounts of the NSD1 proteins. Error bars correspond to the SD of three replicate assays. Input of the HMT reactions is shown in Supplementary Fig. S4c. e Path of the histone H3.3 tail along the SHL1 DNA, the active site and the α2 helix of SETD2. f Detailed view of the active site of SETD2 bound with the K36M mutation.

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