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. 2018 May 25;46(12):6140–6151. doi: 10.1093/nar/gky457

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© The Author(s) 2018. 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 Non-Commercial 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 2. — DnaA-ATP oligomerization is not required for cooperative binding between low affinity sites. (A) EMSA of wild-type DnaA-ATP, DnaA(R285A)-ATP or DnaA-ADP binding to probe carrying the closely spaced sites shown below the panels. DnaA:DNA molar ratios were 0:1, 2.5:1 and 10:1. Positions of unbound probe (0), and probe bound to 1, 2 or 3 molecules of DnaA are marked. (B) DMS footprints of DnaA-ATP, DnaA-ADP and DnaA(R285A)-ATP bound to oriC^allADP. Binding sites and diagnostic G2 and G4 residues are marked. (C) Quantitation of G2 or G4 band intensities for each site when bound to 80 nM DnaA-ATP (gray), DnaA-ADP (black) or DnaA(R285A)-ATP (stippled) relative to intensities at 0 nM DnaA.