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. 2007 May 3;35(10):3407–3419. doi: 10.1093/nar/gkm206

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© 2007 The Author(s)

This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 4. — Synapse assays with wild-type and mutant attB sites. Panel (A) Radiolabelled attP was incubated with wild-type (left panel) or the catalytically inactive integrase, S12A, (right panel) and a cold partner fragment containing wild-type attB (wt) or the indicated mutant attB sites. The arrows show the positions of the synapse containing the radiolabelled substrate, the cold partner fragment and integrase (Int:synapse attP/B), the covalently linked cleaved substrate (Int:cleaved attP/B), the shifted and free products (Int:attL/R and attL/R, respectively) and the positions of the attP bound only to integrase (two complexes labelled Int:attP) or free (attP). Panel (B) The protease subtilisin was used to reveal the extent of cleavage of attB sites and the products formed during the synapse assay. Arrows show the positions of the products, attL and attR, the radiolabelled substrate and attB. The smear of radioactivity migrating faster than the free probe results from subtilisin treated cleaved covalently linked complexes.