Maximilian Seidel, Anja Becker, Filipa Pereira, Jonathan Landry, Jonathan Landry, Nayara Trevisan Doimo de Azevedo, Claudia Mariateresa Fusco, Eva Kaindl, Natalie Romanov, Janina Baumbach, Julian David Langer, Erin M. Schuman, Kiran Raosaheb Patil, Gerhard Hummer, Vladimir Benes, Martin Beck
- 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.
Metadaten| Author: | Maximilian SeidelORCiDGND, Anja Becker, Filipa Pereira, Jonathan LandryORCiDGND, Jonathan LandryORCiDGND, Nayara Trevisan Doimo de Azevedo, Claudia Mariateresa FuscoORCiDGND, Eva Kaindl, Natalie RomanovORCiDGND, Janina Baumbach, Julian David LangerORCiDGND, Erin M. SchumanORCiDGND, Kiran Raosaheb PatilORCiDGND, Gerhard HummerORCiDGND, Vladimir BenesORCiDGND, Martin BeckORCiDGND |
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| URN: | urn:nbn:de:hebis:30:3-632798 |
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| DOI: | https://doi.org/10.1038/s41467-022-28878-5 |
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| ISSN: | 2041-1723 |
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| Parent Title (English): | Nature Communications |
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| Publisher: | Nature Publishing Group UK |
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| Place of publication: | [London] |
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| Document Type: | Article |
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| Language: | English |
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| Date of Publication (online): | 2022/03/09 |
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| Date of first Publication: | 2022/03/09 |
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| Publishing Institution: | Universitätsbibliothek Johann Christian Senckenberg |
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| Release Date: | 2024/08/19 |
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| Tag: | Nuclear pore complex; RNA; RNA sequencing; Translation |
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| Volume: | 13 |
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| Issue: | art. 1224 |
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| Article Number: | 1224 |
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| Page Number: | 15 |
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| First Page: | 1 |
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| Last Page: | 15 |
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| Note: | Data availability
The underlying RIP-qPCR data, uncropped images (e.g. Western Blots, growth assays), polysome profiles, Limma-results, underlying mass spectrometry data and primers which were generated in this study are provided in the Source Data file. The selective ribosome profiling data used in this study are available in the European Nucleotide Archive database under accession code PRJEB46361 and PRJEB50305. The mass spectrometry data generated in this study have been deposited in the PRIDE database under accession codes PXD030626 and PXD028413.
The previously published structures for 4XMM [https://doi.org/10.2210/pdb4XMM/pdb] (Fig. 3a: Seh1-Nup85 dimer within the Nup84 subcomplex), 4BZK [https://doi.org/10.2210/pdb4BZK/pdb] (Fig. 4c, d, f: COPII coat consisting of Sec13-Sec31), 3MZK [https://doi.org/10.2210/pdb3MZK/pdb] (Fig. 4e, f: Sec13-Sec16 complex) and 5CWS [https://doi.org/10.2210/pdb5CWS/pdb] (Figs. 5a and 6a: Central transport Nup-trimer) are accessible at the Protein Data Bank (PDB). The integrative structure of the cytoplasmic filaments21 is available in the PDB-Dev under accession code PDBDEV_00000010 (Fig. 5d). The electron density map of the NPC45 is deposited in the Electron Microscopy Data Bank under accession code EMD-10198 (Fig. 1a). Source data are provided with this paper. |
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| Note: | Code availability
MatLab scripts for analysis and plotting of SeRP data were deposited to Zenodo (https://doi.org/10.5281/zenodo.5887401). The script suite for SeRP58 can be found on Zenodo (https://doi.org/10.5281/zenodo.2602493) and includes the required reference genome files for the coding and non-coding genome of Saccharomyces cerevisiae (R64-1-1). |
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| Note: | Open Access funding enabled and organized by Projekt DEAL. |
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| Note: | Funding: Max Planck Society |
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| Note: | Funding: European Research Council ; 743216 |
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| Note: | Funding: European Research Council ; 724349-ComplexAssembly |
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| Institutes: | Physik |
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| Angeschlossene und kooperierende Institutionen / MPI für Biophysik |
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| Dewey Decimal Classification: | 5 Naturwissenschaften und Mathematik / 53 Physik / 530 Physik |
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| 5 Naturwissenschaften und Mathematik / 57 Biowissenschaften; Biologie / 570 Biowissenschaften; Biologie |
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| Sammlungen: | Universitätspublikationen |
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| Licence (German): |  Creative Commons - CC BY - Namensnennung 4.0 International |
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