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. 2015 May 20;43(12):5824–5837. doi: 10.1093/nar/gkv507

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© The Author(s) 2015. Published by Oxford University Press on behalf of Nucleic Acids Research.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 5. — Nucleosomes favor binding of TRF2^ΔB to adjacent telomeric binding sites. (A) Gel mobility-shift assay. Naked DNA (lanes 1–5) and NCPs (lanes 6–10) were incubated with increasing amounts of TRF2^ΔB. The molar concentration of TRF2^ΔB is indicated above the lanes. Samples were separated on a 0.8% agarose gel. (B) Percentages of unbound DNA and NCPs are reported as a function of protein concentration in the reaction. The concentration of TRF2^ΔB at which 50% of naked DNA and nucleosome remain unbound has been extrapolated.