Sequential domain assembly of ribosomal protein S3 drives 40S subunit maturation.
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.
Mesh Terms:
Fungal Proteins, Gene Expression Regulation, Gene Expression Regulation, Fungal, Models, Molecular, Phosphorylation, Protein Conformation, Protein Subunits, Protein Transport, Ribosomal Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Fungal Proteins, Gene Expression Regulation, Gene Expression Regulation, Fungal, Models, Molecular, Phosphorylation, Protein Conformation, Protein Subunits, Protein Transport, Ribosomal Proteins, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Nat Commun
Date: Feb. 02, 2016
PubMed ID: 26831757
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