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

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. Copyright © 2021 Elsevier Inc. All rights reserved.

Citation

Ophélie Lautier, Arianna Penzo, Jérôme O Rouvière, Guillaume Chevreux, Louis Collet, Isabelle Loïodice, Angela Taddei, Frédéric Devaux, Martine A Collart, Benoit Palancade. Co-translational assembly and localized translation of nucleoporins in nuclear pore complex biogenesis. Molecular cell. 2021 Jun 03;81(11):2417-2427.e5

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PMID: 33838103

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