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

Author

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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)

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.

Suggested Citation

  • Valentin Mitterer & Guillaume Murat & Stéphane Réty & Magali Blaud & Lila Delbos & Tamsyn Stanborough & Helmut Bergler & Nicolas Leulliot & Dieter Kressler & Brigitte Pertschy, 2016. "Sequential domain assembly of ribosomal protein S3 drives 40S subunit maturation," Nature Communications, Nature, vol. 7(1), pages 1-15, April.
    • Handle: RePEc:nat:natcom:v:7:y:2016:i:1:d:10.1038_ncomms10336
    DOI: 10.1038/ncomms10336
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