Extended Data Fig. 3: Detail analysis of the Dot1L-H2BK34ub complex structure.
From: H2B Lys34 Ubiquitination Induces Nucleosome Distortion to Stimulate Dot1L Activity
a, Different view of the 1:1 cryo-EM structure of Dot1L(1-416) bound to the H2BK34ub nucleosome, which contains a string of densities extended from the C terminal of Dot1L(4-332) to the DNA. b, Representative cryo-EM densities of histone H2A/H2B/H3/H4, Dot1L, DNA and ubiquitin. c, Molecular interaction of H2BK120ub and Dot1L. Mutations (I290A, L322A and F326A) that are important for the H2BK120ub nucleosome did not impair the activation of Dot1L by the H2BK34ub nucleosome. Data are presented as mean values ± SD for three biological replicates. d, Close-up view of the interaction between Dot1L and nucleosome. And the methyltransferase activity of WT and different mutant Dot1L constructs. Data are presented as mean values ± SD for three biological replicates.
