Tightly-orchestrated rearrangements govern catalytic center assembly of the ribosome.
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.
Mesh Terms:
Cryoelectron Microscopy, Dual-Specificity Phosphatases, Models, Molecular, Nucleic Acid Conformation, Peptidyl Transferases, Protein Conformation, RNA, Fungal, RNA-Binding Proteins, Ribosomal Proteins, Ribosome Subunits, Large, Eukaryotic, Ribosomes, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Cryoelectron Microscopy, Dual-Specificity Phosphatases, Models, Molecular, Nucleic Acid Conformation, Peptidyl Transferases, Protein Conformation, RNA, Fungal, RNA-Binding Proteins, Ribosomal Proteins, Ribosome Subunits, Large, Eukaryotic, Ribosomes, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins
Nat Commun
Date: Dec. 27, 2018
PubMed ID: 30814529
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