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TitleStructural insights into initial and intermediate steps of the ribosome-recycling process.
Journal, issue, pagesEMBO J, Vol. 31, Issue 7, Page 1836-1846, Year 2012
Publish dateApr 4, 2012
AuthorsTakeshi Yokoyama / Tanvir R Shaikh / Nobuhiro Iwakura / Hideko Kaji / Akira Kaji / Rajendra K Agrawal /
PubMed AbstractThe ribosome-recycling factor (RRF) and elongation factor-G (EF-G) disassemble the 70S post-termination complex (PoTC) into mRNA, tRNA, and two ribosomal subunits. We have determined cryo-electron ...The ribosome-recycling factor (RRF) and elongation factor-G (EF-G) disassemble the 70S post-termination complex (PoTC) into mRNA, tRNA, and two ribosomal subunits. We have determined cryo-electron microscopic structures of the PoTC·RRF complex, with and without EF-G. We find that domain II of RRF initially interacts with universally conserved residues of the 23S rRNA helices 43 and 95, and protein L11 within the 50S ribosomal subunit. Upon EF-G binding, both RRF and tRNA are driven towards the tRNA-exit (E) site, with a large rotational movement of domain II of RRF towards the 30S ribosomal subunit. During this intermediate step of the recycling process, domain II of RRF and domain IV of EF-G adopt hitherto unknown conformations. Furthermore, binding of EF-G to the PoTC·RRF complex reverts the ribosome from ratcheted to unratcheted state. These results suggest that (i) the ribosomal intersubunit reorganizations upon RRF binding and subsequent EF-G binding could be instrumental in destabilizing the PoTC and (ii) the modes of action of EF-G during tRNA translocation and ribosome-recycling steps are markedly different.
External linksEMBO J / PubMed:22388519 / PubMed Central
MethodsEM (single particle)
Resolution9.9 - 11.1 Å
Structure data

1915

3j0d

EMDB-1915: Initial binding position of RRF on the post-termination complex
PDB-3j0d: Models for the T. thermophilus ribosome recycling factor bound to the E. coli post-termination complex
Method: EM (single particle) / Resolution: 11.1 Å

1916

3j0d

EMDB-1916: Initial binding conformation of RRF on the post-termination complex
PDB-3j0d: Models for the T. thermophilus ribosome recycling factor bound to the E. coli post-termination complex
Method: EM (single particle) / Resolution: 11.1 Å

1917

3j0e

EMDB-1917: Intermediate binding positions of RRF and EF-G on the post-termination complex
PDB-3j0e: Models for the T. thermophilus ribosome recycling factor and the E. coli elongation factor G bound to the E. coli post-termination complex
Method: EM (single particle) / Resolution: 9.9 Å

1918

3j0e

EMDB-1918: Binding conformations and positions of RRF and EF-G during intermediate state of ribosome recycling
PDB-3j0e: Models for the T. thermophilus ribosome recycling factor and the E. coli elongation factor G bound to the E. coli post-termination complex
Method: EM (single particle) / Resolution: 9.9 Å

Source
  • escherichia coli (E. coli)
  • thermus thermophilus (bacteria)
KeywordsTRANSLATION / ribosome / ribosome recycling factor / Elongation Factor G

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