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. 2008 Dec 15;183(6):1019–1031. doi: 10.1083/jcb.200801157

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© 2008 Zhang et al.

This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.jcb.org/misc/terms.shtml). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 3.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/3.0/).

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Figure 4. — Fluorescent protein fragment complementation assay showing the Rad21–Rad21 interaction and the antiparallel orientation. (A) YFP(NT) or YFP(CT) were fused to either the NT or CT end of Rad21. YFP-fused Rad21 constructs were expressed in 293T cells (lanes 3–6), and their interaction with the cohesin complex was examined by IP of the endogenous Smc3 using rabbit anti-Smc3 antisera (lanes 9–12). *, nonspecific band. (B) 293T cells were cotransfected with YFP(NT)- and YFP(CT)-fused Rad21 plasmids (a total of four combinations). YFP fluorescence was examined under a fluorescent microscope 40 h after transfection. (C) YFP fluorescence–positive 293T and HeLa cells transfected with the combination of YFP(NT)-Rad21 and Rad21-YFP(CT) at 400× magnification. (D) Possible antiparallel orientation of Rad21–Rad21 interactions. Only the combination of plasmids in the top panel results in the fluorescence. Bars, 25 μm.