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. Author manuscript; available in PMC: 2016 Apr 23.
Published in final edited form as: Cell. 2015 Apr 16;161(3):555–568. doi: 10.1016/j.cell.2015.03.017

Table 1.

Recombinant O, S, K, and M show a range of affinities to nucleosomes. (related to Figure 1)

Oct4 Sox2 Klf4 c-Myc

Apparent Kd (nM) bact. mamm. bact. mamm. bact. mamm. bact. mamm.
total canonical 0.61 0.64 0.37 0.98 2.49 1.46 1.88 ND
specific canonical 0.76 1.04 0.45 1.50 3.18 1.95 0.77 ND
total LIN28B DNA 0.75 0.93 0.38 1.46 1.25 0.41 8.28 ND
specific LIN28B DNA 0.92 2.05 0.68 3.83 2.26 1.12 6.25 ND
total LIN28B nuc. 1.09 1.34 0.34 1.06 5.96 3.45 ND ND
specific LIN28B nuc. 1.17 1.84 0.39 1.43 7.21 13.97 ND ND

Apparent dissociation constants (Kd) were derived from EMSA to represent the relative affinities of bacterial (bact.) and mammalian (mamm.) O, S, K, and M to their canonical sites, LIN28B free DNA, and LIN28B nucleosomes (nuc.). Apparent Kd were derived from two separate binding curves representing two experimental replicates, fitted to the experimental data within R2 values of ~ 0.97, and expressed in nM units. Apparent Kd were quantified from the fractional decrement of free DNA or nuc, designated as “total” binding, or from the first bound-DNA/nuc complexes, representing “specific” binding.