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. Author manuscript; available in PMC: 2010 Jan 23.
Published in final edited form as: Cell. 2009 Jan 23;136(2):284–295. doi: 10.1016/j.cell.2008.11.037

Figure 1. ceNup160 scaffold nucleoporin shows life-long stability.

Figure 1

(A). Scheme of the nuclear pore complex structure and composition. Asterisks denote dynamic nucleoporins. (B) C. elegans N2 wild type strain was injected with a vector expressing GFP under the control of either the ceNup153 promoter or the ceNup160 promoter (Promoter) or with vectors expressing ceNup153-GFP or ceNup160-GFP under their endogenous promoters (full-length protein). Expression of the reporter protein was analyzed by fluorescence microscopy and GFP signal was merged with differential interference contrast images (DIC). Correct localization of ceNup153-GFP and ceNup160-GFP fusion proteins to the NE was analyzed by confocal microscopy (Zoom). (C) The activity of ceNup153 and ceNup160 promoters and the localization of full-length proteins in the head of adult worms were analyzed by confocal microscopy. Image shows the maximal projection of 30 z-stacks. (D) Nuclei were purified from ceNup160-GFP and ceNup153-GFP transgenic worms and NPC insertion of the GFP-tagged nucleoporins (green) was confirmed by colocalization with the NPC antibody mAb414 (red). Chromatin is shown in blue. (E) ceNup153-GFP and ceNup160-GFP expressing worms were subjected to GFP RNAi until no fluorescent signal was detected. RNAi against C. elegans dicer (DCR-1) was used to release adult worms from the GFP RNAi. Adults were fed DCR-1 RNAi for 6 days before the GFP signal was analyzed. Dashed lines outline worms heads.

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