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== Function ==
== Function ==
[https://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B]
[https://www.uniprot.org/uniprot/RL11_ECOLI RL11_ECOLI] This protein binds directly to 23S ribosomal RNA. Forms the L11 stalk, which is mobile in the ribosome, indicating its contribution to the activity of initiation, elongation and release factors.[HAMAP-Rule:MF_00736_B]
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== Publication Abstract from PubMed ==
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.
Structural insights into initial and intermediate steps of the ribosome-recycling process.,Yokoyama T, Shaikh TR, Iwakura N, Kaji H, Kaji A, Agrawal RK EMBO J. 2012 Mar 2;31(7):1836-46. doi: 10.1038/emboj.2012.22. PMID:22388519<ref>PMID:22388519</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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==See Also==
==See Also==
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*[[Ribosome 3D structures|Ribosome 3D structures]]
*[[Ribosome 3D structures|Ribosome 3D structures]]
*[[Ribosome recycling factor|Ribosome recycling factor]]
*[[Ribosome recycling factor|Ribosome recycling factor]]
== References ==
<references/>
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Latest revision as of 10:09, 21 February 2024

Models for the T. thermophilus ribosome recycling factor bound to the E. coli post-termination complex

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