Co-translational assembly orchestrates competing biogenesis pathways

Maximilian Seidel, Anja Becker, Filipa Pereira, Jonathan J. M. Landry, Nayara Trevisan Doimo Azevedo, Claudia M. Fusco, Eva Kaindl, Natalie Romanov, Janina Baumbach, Julian D. Langer, Erin M. Schuman, Kiran Raosaheb Patil, Gerhard Hummer, Vladimir Benes and Martin Beck ()
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Maximilian Seidel: Max Planck Institute of Biophysics
Anja Becker: Max Planck Institute of Biophysics
Filipa Pereira: European Molecular Biology Laboratory (EMBL)
Jonathan J. M. Landry: European Molecular Biology Laboratory (EMBL)
Nayara Trevisan Doimo Azevedo: European Molecular Biology Laboratory (EMBL)
Claudia M. Fusco: Max Planck Institute for Brain Research
Eva Kaindl: Max Planck Institute of Biophysics
Natalie Romanov: Max Planck Institute of Biophysics
Janina Baumbach: Max Planck Institute of Biophysics
Julian D. Langer: Max Planck Institute for Brain Research
Erin M. Schuman: Max Planck Institute for Brain Research
Kiran Raosaheb Patil: European Molecular Biology Laboratory (EMBL)
Gerhard Hummer: Max Planck Institute of Biophysics
Vladimir Benes: European Molecular Biology Laboratory (EMBL)
Martin Beck: Max Planck Institute of Biophysics

Nature Communications, 2022, vol. 13, issue 1, 1-15

Abstract: Abstract 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.

Date: 2022
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-28878-5

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DOI: 10.1038/s41467-022-28878-5

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