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  Co-translational assembly orchestrates competing biogenesis pathways

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.

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 Creators:
Seidel, Maximilian1, 2, Author              
Becker, Anja1, Author              
Pereira, Filipa3, 4, Author
Landry, Jonathan J. M.5, Author
de Azevedo, Nayara Trevisan Doimo5, Author
Fusco, Claudia M.6, Author
Kaindl, Eva1, Author              
Romanov, Natalie1, Author              
Baumbach, Janina1, 3, Author              
Langer, Julian David6, 7, 8, Author              
Schuman, Erin M.6, Author
Patil, Kiran Raosaheb3, 9, Author
Hummer, Gerhard10, 11, Author              
Benes, Vladimir5, Author
Beck, Martin1, 3, Author              
Affiliations:
1Department of Molecular Sociology, Max Planck Institute of Biophysics, Max Planck Society, ou_3040395              
2Faculty of Bioscience, Heidelberg University, Heidelberg, Germany, ou_persistent22              
3Structural and Computational Biology Unit, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany, ou_persistent22              
4Life Sciences Institute, University of Michigan, Ann Arbor, MI, USA, ou_persistent22              
5Genomics Core Facility, European Molecular Biology Laboratory (EMBL), Heidelberg, Germany, ou_persistent22              
6Department of Synaptic Plasticity, Max Planck Institute for Brain Research, Frankfurt, Germany, ou_persistent22              
7Proteomics and Mass Spectrometry, Max Planck Institute of Biophysics, Max Planck Society, ou_3262216              
8Mass Spectrometry, Max Planck Institute for Brain Research, Frankfurt, Germany, ou_persistent22              
9Medical Research Council Toxicology Unit, University of Cambridge, Cambridge, United Kingdom, ou_persistent22              
10Department of Theoretical Biophysics, Max Planck Institute of Biophysics, Max Planck Society, ou_2068292              
11Institute of Biophysics, Goethe University Frankfurt, Frankfurt, Germany, ou_persistent22              

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 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.

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Language(s): eng - English
 Dates: 2021-07-272022-02-112022-03-09
 Publication Status: Published online
 Pages: 15
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1038/s41467-022-28878-5
BibTex Citekey: seidel_co-translational_2022
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Title: Nature Communications
  Abbreviation : Nat. Commun.
Source Genre: Journal
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Publ. Info: London : Nature Publishing Group
Pages: - Volume / Issue: 13 Sequence Number: 1224 Start / End Page: - Identifier: ISSN: 2041-1723
CoNE: https://pure.mpg.de/cone/journals/resource/2041-1723