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dc.contributor.authorSeidel, Maximilian
dc.contributor.authorBecker, Anja
dc.contributor.authorPereira, Filipa
dc.contributor.authorLandry, Jonathan JM
dc.contributor.authorde Azevedo, Nayara Trevisan Doimo
dc.contributor.authorFusco, Claudia M
dc.contributor.authorKaindl, Eva
dc.contributor.authorRomanov, Natalie
dc.contributor.authorBaumbach, Janina
dc.contributor.authorLanger, Julian D
dc.contributor.authorSchuman, Erin M
dc.contributor.authorPatil, Kiran Raosaheb
dc.contributor.authorHummer, Gerhard
dc.contributor.authorBenes, Vladimir
dc.contributor.authorBeck, Martin
dc.date.accessioned2022-03-09T16:02:01Z
dc.date.available2022-03-09T16:02:01Z
dc.date.issued2022-03-09
dc.date.submitted2021-07-27
dc.identifier.issn2041-1723
dc.identifier.others41467-022-28878-5
dc.identifier.other28878
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/334811
dc.descriptionFunder: Max-Planck-Gesellschaft (Max Planck Society); doi: https://doi.org/10.13039/501100004189
dc.description.abstractDuring 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.
dc.languageen
dc.publisherSpringer Science and Business Media LLC
dc.subjectArticle
dc.subject/631/45/500
dc.subject/631/1647/514/1949
dc.subject/631/80/389/2029
dc.subject/631/337/574
dc.subject/38/91
dc.subject/38/88
dc.subject/38/90
dc.subject/82/58
dc.subjectarticle
dc.titleCo-translational assembly orchestrates competing biogenesis pathways.
dc.typeArticle
dc.date.updated2022-03-09T16:02:00Z
prism.issueIdentifier1
prism.publicationNameNat Commun
prism.volume13
dc.identifier.doi10.17863/CAM.82243
dcterms.dateAccepted2022-02-11
rioxxterms.versionofrecord10.1038/s41467-022-28878-5
rioxxterms.versionVoR
rioxxterms.licenseref.urihttp://creativecommons.org/licenses/by/4.0/
dc.contributor.orcidSeidel, Maximilian [0000-0003-1615-3549]
dc.contributor.orcidFusco, Claudia M [0000-0002-9812-2203]
dc.contributor.orcidLanger, Julian D [0000-0002-5190-577X]
dc.contributor.orcidSchuman, Erin M [0000-0001-7505-1855]
dc.contributor.orcidHummer, Gerhard [0000-0001-7768-746X]
dc.contributor.orcidBenes, Vladimir [0000-0002-0352-2547]
dc.contributor.orcidBeck, Martin [0000-0002-7397-1321]
dc.identifier.eissn2041-1723
pubs.funder-project-idEC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) (724349, 743216)
cam.issuedOnline2022-03-09


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