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. 2012 Sep 8;40(20):10215–10227. doi: 10.1093/nar/gks747

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© The Author(s) 2012. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 2. — DNA sequence does not influence H3(K56ac) enhancement of TF binding. (A) Cy3 fluorescence image of native PAGE analysis of purified FRET-labeled nucleosomes containing the 5SL NPS and unmodified H3 (lane 2), H3(K56Q) (lane 3) or H3(K56ac) (lane 4). (B and C) Fluoresence emission spectra of 5SL FRET-labeled nucleosomes containing unmodified H3 or H3(K56ac), respectively, excited at 510 nm (donor excitation) in the presence of 0.5× TE, 1 mM NaCl and LexA at 0 nM (black), 30 nM (red) or 1000 nM (blue), (D) Steady-state FRET efficiency, as determined by the (ratio)_A method (36), versus LexA concentration for nucleosomes containing unmodified H3 (blue), H3(C110) (purple), H3(K56Q) (red), and H3(K56a) (orange) at 1 mM NaCl. Plots are the average of three LexA titrations and the error bars were determined from the SD of the three measurements. The data were fit to a non-cooperative binding curve, which determines S_0.5-nuc, the LexA concentration at which 50% of the nucleosomes are bound by LexA. (E) Relative change in K_eq for nucleosomes with the 601L (14) or 5SL NPS containing H3(K56Q) or H3(K56ac) versus unmodified H3 at 1 mM NaCl. This is inversely related to the relative change in S_0.5.