Fig. 2: Paralogues linker Nups co-translationally engage with their binding partners.
From: Co-translational assembly orchestrates competing biogenesis pathways
a Primary structure scheme of the paralogous FG-Nups Nup145N, Nup116 and Nup100. b RIP-qPCR experiments with affinity purified Gle2 that show co-translational binding to nascent Nup116. n = 4 biologically independent samples for Gle2-StepII (gle2-, nup100-, nup116-, and nup145-mRNA). *p = 0.0143 for Gle2-StepII (nup116-mRNA). RIP-qPCR was used to characterize co-translational interactions between c, Nup192 and Nup100 d, Nup157 and Nup170 with linker Nups and e Nup116 and Nup82. n = 5 biologically independent samples for Nup192-StepII (nup116- and nup145-mRNA), Nup116-StepII (nup82-mRNA) and Nup82-StepII (nup116-mRNA); n = 4 biologically independent samples for Nup192-StepII (nup100-mRNA), Nup100-StepII (nup192-mRNA), Nup157-StrepII (nup100-, nup116- and nup145-mRNA) and Nup170-StrepII (nup100-, nup116- and nup145-mRNA). **p = 0.0023 for Nup157-StepII (nup145-mRNA) and *p = 0.0296 for Nup116-StepII (nup82-mRNA). f Scheme highlighting that designated assembly pathways may exist for paralogs. Bar graphs in panel b–e depict mean ± SD. ns p > 0.05,* p < 0.05, ** p < 0.01 (Two-sided, paired t-test). Source data for RIP-qPCR in panel b–e, are provided as a Source Data file. AA amino acid, IP immunoprecipitation, FG phenylalanine-glycine repeats, MD middle domain, APD autoproteolytic domain.
