Fig. 5: Nascent chaperoning and cargo complex formation of r-proteins.
From: Co-translational binding of importins to nascent proteins
SeRP profiles and AlphaFold models of (a) Rps5, (b) Rpl18a, and (c) Rpl28. a, b The SeRP profiles reveal, that for nascent Rps5 and Rpl18a, Ssb1 first binds to the nascent chain. Subsequently, it is released prior to Kap123 binding. c In contrast, Rpl28 does not require Ssb1 chaperoning. Nevertheless, Kap123 binds C-terminally. The folds exemplify the structural organization of many r-proteins. A nascent r-protein recognized by Kap123 contains an N-terminally disordered, charged patch and a consecutive structured domain. SeRP profiles (IP/total) are shown for the respective mRNA targets from n = 4 biologically independent replicates (solid lines are averaged across replicates; shades reflect largest to smalls replicate value interval). Gray dashed lines indicate an arbitrary threshold of 2 used for onset estimation. SeRP for Ssb117 represents profiles generated from n = 2 biologically independent replicates. AlphaFold models of r-proteins were obtained from the AlphaFold database (https://alphafold.ebi.ac.uk/)83,84. C-terminal binding sites (40 AA downstream of onset) are labeled for Ssb1 and Kap123 within the structures, respectively. IP immunoprecipitation, AA amino acid.
