Sequential domain assembly of ribosomal protein S3 drives 40S subunit maturation

Valentin Mitterer, Guillaume Murat, Stéphane Réty, Magali Blaud, Lila Delbos, Tamsyn Stanborough, Helmut Bergler, Nicolas Leulliot (), Dieter Kressler () and Brigitte Pertschy ()
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Valentin Mitterer: Institut für Molekulare Biowissenschaften, Universität Graz
Guillaume Murat: Unit of Biochemistry, University of Fribourg
Stéphane Réty: Laboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Pharmacie
Magali Blaud: Laboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Pharmacie
Lila Delbos: Laboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Pharmacie
Tamsyn Stanborough: Institut für Molekulare Biowissenschaften, Universität Graz
Helmut Bergler: Institut für Molekulare Biowissenschaften, Universität Graz
Nicolas Leulliot: Laboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Pharmacie
Dieter Kressler: Unit of Biochemistry, University of Fribourg
Brigitte Pertschy: Institut für Molekulare Biowissenschaften, Universität Graz

Nature Communications, 2016, vol. 7, issue 1, 1-15

Abstract: Abstract 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.

Date: 2016
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DOI: 10.1038/ncomms10336

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