EMD-2010
3D reconstruction of a translating yeast 80S ribosome in complex with Dom34p and Rli1p
EMD-2010
Single-particle7.2 Å
Deposition: 12/12/2011Map released: 17/02/2012
Last modified: 01/03/2012
Sample Organism:
Saccharomyces cerevisiae
Sample: Saccharomyces cerevisiae 80S ribosome stalled by a synthetic stem-loop mRNA in complex with Dom34p and Rli1p
Fitted models: 3j16 (Avg. Q-score: 0.118)
Deposition Authors: Becker T, Franckenberg S, Wickles S, Shoemaker CJ, Anger AM, Armache J-P, Sieber H, Ungewickell C, Berninghausen O, Daberkow I, Karcher A, Thomm M, Hopfner K-P, Green R, Beckmann R
Sample: Saccharomyces cerevisiae 80S ribosome stalled by a synthetic stem-loop mRNA in complex with Dom34p and Rli1p
Fitted models: 3j16 (Avg. Q-score: 0.118)
Deposition Authors: Becker T, Franckenberg S, Wickles S, Shoemaker CJ, Anger AM, Armache J-P, Sieber H, Ungewickell C, Berninghausen O, Daberkow I, Karcher A, Thomm M, Hopfner K-P, Green R, Beckmann R
Structural basis of highly conserved ribosome recycling in eukaryotes and archaea.
Becker T,
Franckenberg S,
Wickles S,
Shoemaker CJ,
Anger AM,
Armache JP 
,
Sieber H,
Ungewickell C,
Berninghausen O,
Daberkow I,
Karcher A,
Thomm M,
Hopfner KP ,
Green R,
Beckmann R
(2012) Nature , 482 , 501 - 506
,
Sieber H,
Ungewickell C,
Berninghausen O,
Daberkow I,
Karcher A,
Thomm M,
Hopfner KP ,
Green R,
Beckmann R
(2012) Nature , 482 , 501 - 506
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.
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.