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-Structure paper
Title | Tightly-orchestrated rearrangements govern catalytic center assembly of the ribosome. |
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Journal, issue, pages | Nat Commun, Vol. 10, Issue 1, Page 958, Year 2019 |
Publish date | Feb 27, 2019 |
Authors | Yi Zhou / Sharmishtha Musalgaonkar / Arlen W Johnson / David W Taylor / |
PubMed Abstract | 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 ...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. |
External links | Nat Commun / PubMed:30814529 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.5 - 3.8 Å |
Structure data | EMDB-0369, PDB-6n8j: EMDB-0370, PDB-6n8k: EMDB-0371, PDB-6n8l: EMDB-0372, PDB-6n8m: |
Chemicals | ChemComp-GTP: ChemComp-MG: |
Source |
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Keywords | RIBOSOME / ribosome biogenesis / Nmd3 / peptidyl transferase center |