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. Author manuscript; available in PMC: 2015 Apr 29.
Published in final edited form as: Nature. 2014 Oct 30;514(7524):591–596. doi: 10.1038/nature13890

Figure 3. UbcH5c binds to nucleosomal DNA enhancing Ring1B/Bmi1-NCP affinity.

Figure 3

a, UbcH5c antiparallel β-sheet-DNA end interactions. Important phosphates colored pink. The catalytic UbcH5c Cys85 is shown. b, UbcH5c-dyad interactions. The nucleosome dyad nucleotide is colored purple. Arg72 and Lys128 side chains not modeled due to limited electron density. c, Fluorescence quenching NCP binding curves for E3 Ring1B/Bmi1 alone (grey), fused to E2 UbcH5c (black), or with E2 UbcH5c added in trans (colored as shown). E2 UbcH5c alone (open squares) is undetectable under assay conditions as it either fails to bind to the NCP or is undetectable due to the location of the fluorescent probe used to monitor Ring1B/Bmi1 binding. Means and standard deviations are shown with n = 3 for each data point. Fluorescence is normalized to fit values for unbound and saturated NCP. Concentrations depicted using log scale.