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Co-translational assembly orchestrates competing biogenesis pathways.

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Becker, Anja 
Pereira, Filipa 
Landry, Jonathan JM 
de Azevedo, Nayara Trevisan Doimo 


During the co-translational assembly of protein complexes, a fully synthesized subunit engages with the nascent chain of a newly synthesized interaction partner. Such events are thought to contribute to productive assembly, but their exact physiological relevance remains underexplored. Here, we examine structural motifs contained in nucleoporins for their potential to facilitate co-translational assembly. We experimentally test candidate structural motifs and identify several previously unknown co-translational interactions. We demonstrate by selective ribosome profiling that domain invasion motifs of beta-propellers, coiled-coils, and short linear motifs may act as co-translational assembly domains. Such motifs are often contained in proteins that are members of multiple complexes (moonlighters) and engage with closely related paralogs. Surprisingly, moonlighters and paralogs assemble co-translationally in only some but not all of the relevant biogenesis pathways. Our results highlight the regulatory complexity of assembly pathways.


Funder: Max-Planck-Gesellschaft (Max Planck Society); doi:


Article, /631/45/500, /631/1647/514/1949, /631/80/389/2029, /631/337/574, /38/91, /38/88, /38/90, /82/58, article

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Nat Commun

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EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) (724349, 743216)