Structural basis of highly conserved ribosome recycling in eukaryotes and archaea

Thomas Becker, Sibylle Franckenberg, Stephan Wickles, Christopher J. Shoemaker, Andreas M. Anger, Jean Paul Armache, Heidemarie Sieber, Charlotte Ungewickell, Otto Berninghausen, Ingo Daberkow, Annette Karcher, Michael Thomm, Karl Peter Hopfner, Rachel Green, Roland Beckmann

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Abstract

Ribosome-driven protein biosynthesis is comprised of four phases: initiation, elongation, termination and recycling. In bacteria, ribosome recycling requires ribosome recycling factor and elongation factor G, and several structures of bacterial recycling complexes have been determined. In the eukaryotic and archaeal kingdoms, however, recycling involves the ABC-type ATPase ABCE1 and little is known about its structural basis. Here we present cryo-electron microscopy reconstructions of eukaryotic and archaeal ribosome recycling complexes containing ABCE1 and the termination factor paralogue Pelota. These structures reveal the overall binding mode of ABCE1 to be similar to canonical translation factors. Moreover, the iron-sulphur cluster domain of ABCE1 interacts with and stabilizes Pelota in a conformation that reaches towards the peptidyl transferase centre, thus explaining how ABCE1 may stimulate peptide-release activity of canonical termination factors. Using the mechanochemical properties of ABCE1, a conserved mechanism in archaea and eukaryotes is suggested that couples translation termination to recycling, and eventually to re-initiation.

Original languageEnglish (US)
Pages (from-to)501-506
Number of pages6
JournalNature
Volume482
Issue number7386
DOIs
StatePublished - Feb 23 2012

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Becker, T., Franckenberg, S., Wickles, S., Shoemaker, C. J., Anger, A. M., Armache, J. P., Sieber, H., Ungewickell, C., Berninghausen, O., Daberkow, I., Karcher, A., Thomm, M., Hopfner, K. P., Green, R., & Beckmann, R. (2012). Structural basis of highly conserved ribosome recycling in eukaryotes and archaea. Nature, 482(7386), 501-506. https://doi.org/10.1038/nature10829