title: Sequential domain assembly of ribosomal protein S3 drives 40S subunit maturation.
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.
authors.affiliation: Institut für Molekulare Biowissenschaften, Universität Graz, Humboldtstrasse 50, 8010 Graz, Austria.
authors.forename: Valentin
authors.initials: V
authors.lastname: Mitterer
authors.affiliation: Unit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, CH-1700 Fribourg, Switzerland.
authors.forename: Guillaume
authors.initials: G
authors.lastname: Murat
authors.affiliation: Laboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Pharmacie, 75006 Paris, France.
authors.forename: Stéphane
authors.initials: S
authors.lastname: Réty
authors.affiliation: Laboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Pharmacie, 75006 Paris, France.
authors.forename: Magali
authors.initials: M
authors.lastname: Blaud
authors.affiliation: Laboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Pharmacie, 75006 Paris, France.
authors.forename: Lila
authors.initials: L
authors.lastname: Delbos
authors.affiliation: Institut für Molekulare Biowissenschaften, Universität Graz, Humboldtstrasse 50, 8010 Graz, Austria.
authors.forename: Tamsyn
authors.initials: T
authors.lastname: Stanborough
authors.affiliation: Institut für Molekulare Biowissenschaften, Universität Graz, Humboldtstrasse 50, 8010 Graz, Austria.
authors.forename: Helmut
authors.initials: H
authors.lastname: Bergler
authors.affiliation: Laboratoire de Cristallographie et RMN Biologiques, UMR CNRS 8015, Université Paris Descartes, Sorbonne Paris Cité, Faculté de Pharmacie, 75006 Paris, France.
authors.forename: Nicolas
authors.identifier: http://orcid.org/0000-0003-0283-4298
authors.initials: N
authors.lastname: Leulliot
authors.affiliation: Unit of Biochemistry, Department of Biology, University of Fribourg, Chemin du Musée 10, CH-1700 Fribourg, Switzerland.
authors.forename: Dieter
authors.initials: D
authors.lastname: Kressler
authors.affiliation: Institut für Molekulare Biowissenschaften, Universität Graz, Humboldtstrasse 50, 8010 Graz, Austria.
authors.forename: Brigitte
authors.initials: B
authors.lastname: Pertschy
mesh_terms: D005656:Fungal Proteins / Q000235:genetics / Q000378:metabolism; D005786:Gene Expression Regulation / Q000502:physiology*; D015966:Gene Expression Regulation, Fungal / Q000502:physiology; D008958:Models, Molecular; D010766:Phosphorylation; D011487:Protein Conformation; D021122:Protein Subunits; D021381:Protein Transport; D012269:Ribosomal Proteins / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000235:genetics / Q000378:metabolism*; D029701:Saccharomyces cerevisiae Proteins / Q000235:genetics / Q000378:metabolism*
chemical_list: D005656:Fungal Proteins; C501335:LTV1 protein, S cerevisiae; D021122:Protein Subunits; C501334:RPS3 protein, S cerevisiae; D012269:Ribosomal Proteins; D029701:Saccharomyces cerevisiae Proteins; C099981:YAR1 protein, S cerevisiae
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