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

Ophélie Lautier, Arianna Penzo, Jérôme O Rouvière, Guillaume Chevreux, Louis Collet, Isabelle Loïodice, Angela Taddei, Frédéric Devaux, Martine A Collart, Benoit Palancade

Molecular cell 2021 Jun 03

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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