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. 2015 Jan 20;6(1):40–54. doi: 10.1080/19491034.2015.1004260

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© 2015 The Author(s). Published with license by Taylor & Francis Group, LLC

© Michal Schwartz, Anna Travesa, Steven W Martell, and Douglass J Forbes

This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted.

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Figure 6. — Nup133 N- and C-terminal protein fragments bind nucleoporins differentially. (A) Full length human Nup133 (1141 aa) and specific mapped domains are shown. The N-terminal, designated Nt-Nup133, consisted of 805 aa and contained the β-propeller domain, the ALPS motif, and a portion of the α-helical domain. The C-terminal Ct-Nup133 construct consisted of aa 917–1141 and contained the site for Nup107 interaction (aa 934–980). (B–C) U20S 2–6–3 cells were transfected with the designated Nup133 fragment. The extent of nucleoporin recruitment was then tested by staining with anti-LacI antibody together with antibodies to Nup160 (B-C) or Pom121, ELYS, Nup53, Nup98, and Nup214 (D). The percentage of transfected cells showing rim localization is shown in last column of (D). The comparative data for full length Nup133 is presented in Table 1.