Fig. 3: Beta-propellers can be complemented co-translationally in vivo.
From: Co-translational assembly orchestrates competing biogenesis pathways
a Crystal structure of Seh1 bound to Nup85 (PDB: 4XMM)49. b RIP-qPCR reveals co-translational entanglement of Seh1 with Nup85. Bar graphs show mean ± SD. n = 6 biologically independent samples for Seh1-StepII (seh1- and nup85-mRNA) and Nup85-StepII (seh1- and nup85-mRNA) and n = 4 biologically independent samples for Seh1-StepII (sea4-mRNA). *p = 0.0178 for Seh1-StepII (seh1-mRNA) and **p = 0.0065 for Seh1-StepII (nup85-mRNA). c Selective ribosome profiling data derived from a Seh1-IP shows that helices at the trunk of Nup85 but not the domain invasion motif (WD40-domain), are required for stable association with Seh1. Selective ribosome profiling was performed with n = 4 biologically independent replicates. d Seh1 might restrict the flexibility of the alpha-solenoid by binding to a structural joint represented by the helices it attaches to. ns p > 0.05, *p < 0.05, ** p < 0.01 (Two-sided, paired t-test). Source data for RIP-qPCR in panel b, are provided as a Source Data file. AA amino acid, IP immunoprecipitation, NPC nuclear pore complex.
