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Co-translational assembly orchestrates competing biogenesis pathways

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Seidel,  Maximilian
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;
Faculty of Bioscience, Heidelberg University, Heidelberg, Germany;

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Becker,  Anja
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;

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Kaindl,  Eva
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;

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Romanov,  Natalie
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;

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Baumbach,  Janina
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;
Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany;

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Langer,  Julian David
Department of Synaptic Plasticity, Max Planck Institute for Brain Research, Frankfurt, Germany;
Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society;
Mass Spectrometry, Max Planck Institute for Brain Research, Frankfurt, Germany;

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Hummer,  Gerhard
Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society;
Institute of Biophysics, Goethe University Frankfurt, Frankfurt, Germany;

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Beck,  Martin
Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society;
Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany;

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Citation

Seidel, M., Becker, A., Pereira, F., Landry, J. J. M., de Azevedo, N. T. D., Fusco, C. M., et al. (2022). Co-translational assembly orchestrates competing biogenesis pathways. Nature Communications, 13: 1224. doi:10.1038/s41467-022-28878-5.


Cite as: https://hdl.handle.net/21.11116/0000-000A-17E5-A
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.