Structural Basis of Highly Conserved Ribosome Recycling in Eukaryotes and Archaea

Overview

Journal Nature

Specialty Science

Date 2012 Feb 24

PMID 22358840

Citations 127

Authors

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

Affiliations

Soon will be listed here.

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.

Citing Articles

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