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Integrity of the P-site is probed during maturation of the 60S ribosomal subunit.

http://www.ncbi.nlm.nih.gov/pubmed/22689654

Eukaryotic ribosomes are preassembled in the nucleus and mature in the cytoplasm. Release of the antiassociation factor Tif6 by the translocase-like guanosine triphosphatase Efl1 is a critical late maturation step. In this paper, we show that a loop of Rpl10 that embraces the P-site transfer ribonucleic acid was required for release of Tif6, 90 Å away. Mutations in this P-site loop blocked 60S maturation but were suppressed by mutations in Tif6 or Efl1. Molecular dynamics simulations of the mutant Efl1 proteins suggest that they promote a conformation change in Efl1 equivalent to changes that elongation factor G and eEF2 undergo during translocation. These results identify molecular signaling from the P-site to Tif6 via Efl1, suggesting that the integrity of the P-site is interrogated during maturation. We propose that Efl1 promotes a functional check of the integrity of the 60S subunit before its first round of translation.

Pubmed ID: 22689654 RIS Download

Mesh terms: Catalytic Domain | Cell Nucleus | GTP Phosphohydrolases | Models, Molecular | Molecular Dynamics Simulation | Mutation | Protein Conformation | RNA, Messenger | Ribosomal Proteins | Ribosome Subunits, Large, Eukaryotic | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins

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Associated grants

  • Agency: NIGMS NIH HHS, Id: GM53655
  • Agency: NIGMS NIH HHS, Id: R01 GM029169
  • Agency: NIGMS NIH HHS, Id: R01 GM29169
  • Agency: Howard Hughes Medical Institute, Id:

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