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 and Roland Beckmann ()
Additional contact information
Thomas Becker: Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany
Sibylle Franckenberg: Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany
Stephan Wickles: Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany
Christopher J. Shoemaker: Howard Hughes Medical Institute, Johns Hopkins University School of Medicine
Andreas M. Anger: Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany
Jean-Paul Armache: Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany
Heidemarie Sieber: Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany
Charlotte Ungewickell: Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany
Otto Berninghausen: Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany
Ingo Daberkow: Tietz Video and Image Processing Systems GmbH, Eremitenweg 1
Annette Karcher: Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany
Michael Thomm: NWF III/Biology and Preclinical Medicine, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany
Karl-Peter Hopfner: Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany
Rachel Green: Howard Hughes Medical Institute, Johns Hopkins University School of Medicine
Roland Beckmann: Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany

Nature, 2012, vol. 482, issue 7386, 501-506

Abstract: 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.

Date: 2012
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DOI: 10.1038/nature10829

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