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. 2014 Feb 6;111(7):2530–2535. doi: 10.1073/pnas.1311081111

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Fig. 4. — Biochemical interaction analysis. (A) Domain organization of ctNup53 and ctNic96. C, C-terminal segment; H, amphipathic helix; H1, Helix 1; H2, Helix 2; N, N-terminal segment; RRM, RNA-recognition motif domain; U, unstructured segment. Black bars highlight fragments used for interaction analysis. SEC analysis of ctNup192^NTD with ctNup53^N (B) or ctNic96^H2 (C). SEC analysis of ctNup192^CTD with ctNup53^N (D) or ctNic96^H2 (E). (F) SEC analysis of Kap-α with ctNup53^N. (G) SEC analysis of competitive binding between Kap-α•ctNup53^N and ctNup192^NTD. Gray bars and colored lines designate the analyzed fractions in the respective SDS/PAGE gels stained with Coomassie brilliant blue (Fig. S5 B–E, G, and H).