Tightly-orchestrated rearrangements govern catalytic center assembly of the ribosome

• Published in: Nature communications Vol. 10; no. 1; p. 958
• Main Authors: Zhou, Yi, Musalgaonkar, Sharmishtha, Johnson, Arlen W, Taylor, David W
• Format: Journal Article
• Language: English
• Published: England Nature Publishing Group 27.02.2019; Nature Publishing Group UK; Nature Portfolio
• Subjects: Amino acid sequence; Assembly; Binding sites; Biosynthesis; Catalysis; Catalytic activity; Cryoelectron Microscopy; Cytoplasm; Dual-Specificity Phosphatases - chemistry; Dual-Specificity Phosphatases - metabolism; Eukaryotes; Insertion; Intermediates; Ligands; Models, Molecular; Nucleic Acid Conformation; Nucleotide sequence; Peptidyl Transferases - chemistry; Peptidyl Transferases - metabolism; Polypeptides; Protein Conformation; Proteins; Ribonucleic acid; Ribosomal Proteins - chemistry; Ribosomal Proteins - metabolism; Ribosome Subunits, Large, Eukaryotic - chemistry; Ribosome Subunits, Large, Eukaryotic - metabolism; Ribosome Subunits, Large, Eukaryotic - ultrastructure; Ribosomes - chemistry; Ribosomes - metabolism; Ribosomes - ultrastructure; RNA; RNA, Fungal - chemistry; RNA, Fungal - metabolism; RNA-Binding Proteins - chemistry; RNA-Binding Proteins - metabolism; Saccharomyces cerevisiae - metabolism; Saccharomyces cerevisiae - ultrastructure; Saccharomyces cerevisiae Proteins - chemistry; Saccharomyces cerevisiae Proteins - metabolism
• ISSN: 2041-1723; 2041-1723
• DOI: 10.1038/s41467-019-08880-0

The catalytic activity of the ribosome is mediated by RNA, yet proteins are essential for the function of the peptidyl transferase center (PTC). In eukaryotes, final assembly of the PTC occurs in the cytoplasm by insertion of the ribosomal protein Rpl10 (uL16). We determine structures of six intermediates in late nuclear and cytoplasmic maturation of the large subunit that reveal a tightly-choreographed sequence of protein and RNA rearrangements controlling the insertion of Rpl10. We also determine the structure of the biogenesis factor Yvh1 and show how it promotes assembly of the P stalk, a critical element for recruitment of GTPases that drive translation. Together, our structures provide a blueprint for final assembly of a functional ribosome.