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. 2014 Jun 9;42(12):7833–7850. doi: 10.1093/nar/gku488

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© The Author(s) 2014. 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/3.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Figure 8. — U2AF65–U2AF35 interaction is essential for Jmjd6 complex formation. Interaction of the U2AF-heterodimer is based on recognition of a specific tryptophane finger motif in U2AF65 by a modified RRM of U2AF35 (45). Mutation of the U2AF35 binding site in U2AF65 (U2AF65-mutTrp: W92A, P96G, P104G) inhibited the co-immunoprecipitation of HA-tagged U2AF65-mutTrp by GFP-tagged U2AF35 (A). In contrast, GFP-tagged Jmjd6 is able to pull down both, wildtype and mutTrp U2AF65 (B). Lysates of 293T cells overexpressing Jmjd6 (pcDNA3), U2AF35-GFP and either wildtype HA-tagged U2AF65 (lane 1) or HA-tagged U2AF65-mutTrp (lane 2) were separated on a native gel (C). As in Figure 7 two bands show co-migration of Jmjd6 with U2AF65 (red, green and yellow double arrows, left hand panel. (1) The slower migrating band contains U2AF35 (right hand panel, 1). With U2AF65-mutTrp the U2AF35-containing band is not present (both panels, (2) a trimeric U2AF65–U2AF35–Jmjd6 complex is not observed with U2AF65-mutTrp.