Mitterer, Valentin Murat, Guillaume Réty, Stéphane Blaud, Magali Delbos, Lila Stanborough, Tamsyn Bergler, Helmut Leulliot, Nicolas Kressler, Dieter Pertschy, Brigitte 2016-02-02 Eukaryotic ribosomes assemble by association of ribosomal RNA with ribosomal proteins into nuclear precursor particles, which undergo a complex maturation pathway coordinated by non-ribosomal assembly factors. Here, we provide functional insights into how successive structural re-arrangements in ribosomal protein S3 promote maturation of the 40S ribosomal subunit. We show that S3 dimerizes and is imported into the nucleus with its N-domain in a rotated conformation and associated with the chaperone Yar1. Initial assembly of S3 with 40S precursors occurs via its C- domain, while the N-domain protrudes from the 40S surface. Yar1 is replaced by the assembly factor Ltv1, thereby fixing the S3 N-domain in the rotated orientation and preventing its 40S association. Finally, Ltv1 release, triggered by phosphorylation, and flipping of the S3 N-domain into its final position results in the stable integration of S3. Such a stepwise assembly may represent a new paradigm for the incorporation of ribosomal proteins. application/pdf https://folia.unifr.ch/global/documents/304783 https://folia.unifr.ch/documents/304783/files/kre_sda.pdf https://folia.unifr.ch/documents/304783/files/kre_sda_sm.pdf eng info:eu-repo/semantics/altIdentifier/doi/10.1038/ncomms10336 info:eu-repo/semantics/openAccess License undefined Nature Communications. - 2016, vol. 7, p. 10336 info:eu-repo/classification/udc/57 Sequential domain assembly of ribosomal protein S3 drives 40S subunit maturation http://purl.org/coar/resource_type/c_6501