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

• DOI: 10.1038/ncomms10336
• Publication Date: 2016-02-02T11:23:24Z
• Authors: Valentin Mitterer; Guillaume Murat; Stéphane Réty; Magali Blaud; Lila Delbos; Tamsyn Stanborough; Helmut Bergler; Nicolas Leulliot; Dieter Kressler; Brigitte Pertschy
• Keywords: Ribosomal protein; 30S; Eukaryotic Ribosome

Abstract Eukaryotic ribosomes assemble by association of ribosomal RNA with proteins into nuclear precursor particles, which undergo a complex maturation pathway coordinated non-ribosomal assembly factors. Here, we provide functional insights how successive structural re-arrangements in protein S3 promote the 40S subunit. We show that dimerizes and is imported nucleus its N-domain rotated conformation associated chaperone Yar1. Initial precursors occurs via C-domain, while protrudes from surface. Yar1 replaced factor Ltv1, thereby fixing orientation preventing association. Finally, Ltv1 release, triggered phosphorylation, flipping final position results stable integration S3. Such stepwise may represent new paradigm for incorporation proteins.