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. 2017 Jan 13;45(6):3591–3605. doi: 10.1093/nar/gkw1356

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© The Author(s) 2017. 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-nc/4.0/), which permits non-commercial re-use, distribution, and reproduction in any medium, provided the original work is properly cited. For commercial re-use, please contact journals.permissions@oup.com

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Figure 3. — DNA binding and cleavage exhibit identical protein concentration dependence. (A) At room temperature, full length TerL^P74-26 binds DNA at concentrations greater than 2 μM (no SDS added to the samples). DNA migrates slower, indicating greater binding, as the TerL^P74-26 concentration is raised. (B) At 60°C, TerL^P74-26 cleaves DNA proportional to the degree of DNA binding observed at room temperature. Tighter binding (slower migration) at room temperature corresponds with more complete DNA digestion at 60°C.