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Co-translational assembly and localized translation of nucleoporins in nuclear pore complex biogenesis.

TitleCo-translational assembly and localized translation of nucleoporins in nuclear pore complex biogenesis.
Publication TypeJournal Article
Year of Publication2021
AuthorsLautier, O, Penzo, A, Rouviere, JO, Chevreux, G, Collet, L, Loïodice, I, Taddei, A, Devaux, F, Collart, MA, Palancade, B
JournalMol Cell
Date Published2021 Apr 04
ISSN1097-4164
Abstract

mRNA translation is coupled to multiprotein complex assembly in the cytoplasm or to protein delivery into intracellular compartments. Here, by combining systematic RNA immunoprecipitation and single-molecule RNA imaging in yeast, we have provided a complete depiction of the co-translational events involved in the biogenesis of a large multiprotein assembly, the nuclear pore complex (NPC). We report that binary interactions between NPC subunits can be established during translation, in the cytoplasm. Strikingly, the nucleoporins Nup1/Nup2, together with a number of nuclear proteins, are instead translated at nuclear pores, through a mechanism involving interactions between their nascent N-termini and nuclear transport receptors. Uncoupling this co-translational recruitment further triggers the formation of cytoplasmic foci of unassembled polypeptides. Altogether, our data reveal that distinct, spatially segregated modes of co-translational interactions foster the ordered assembly of NPC subunits and that localized translation can ensure the proper delivery of proteins to the pore and the nucleus.

DOI10.1016/j.molcel.2021.03.030
Alternate JournalMol Cell
PubMed ID33838103

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