Ribosome recycling revisited |
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Authors: | O Vesper D N Wilson |
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Institution: | (1) MPI Molekulare Genetik, AG Ribosomen Ihnestr. 73, Berlin, D-14195, Germany |
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Abstract: | Ribosome recycling involves the coordinated action of the ribosome recycling factor (RRF), elongation factor EF-G, and the
initiation factor IF3 to disassemble the posttermination complex, recycling the components for the next round of translation.
The crystal structure of domain I of RRF (RRF-DI) in complex with the large ribosomal subunit from the eubacteria Deinococcus radiodurans at a high resolution reveals the nature and details of the interactions between this protein factor and the rRNA/protein
components of the ribosome. Universally conserved arginine residues within the RRF-DI establish important interactions with
nucleotides of the 23S rRNA, thus explaining why mutations at these positions abolish factor binding. Furthermore, in conjunction
with cryo-EM reconstruction, the X-ray analysis provides a structural complement to the recent biochemical data, offering
additional insight into the mechanism of ribosome recycling.
Published in Russian in Molekulyarnaya Biologiya, 2006, Vol. 40, No. 4, pp. 742–750.
The text was submitted by the authors in English. |
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Keywords: | ribosome rRNA ribosomal protein ribosome recycling factor RRF Trigger factor Tf |
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