TY - JOUR
T1 - Structural basis of highly conserved ribosome recycling in eukaryotes and archaea
AU - Becker, Thomas
AU - Franckenberg, Sibylle
AU - Wickles, Stephan
AU - Shoemaker, Christopher J.
AU - Anger, Andreas M.
AU - Armache, Jean Paul
AU - Sieber, Heidemarie
AU - Ungewickell, Charlotte
AU - Berninghausen, Otto
AU - Daberkow, Ingo
AU - Karcher, Annette
AU - Thomm, Michael
AU - Hopfner, Karl Peter
AU - Green, Rachel
AU - Beckmann, Roland
N1 - Funding Information:
Acknowledgements We thank A. Schele and A. Gilmozzi for technical assistance, and D. Wilson for critical discussions. This work was supported by grants from the Deutsche Forschungsgemeinschaft, SFB594 (to R.B.), SFB646 (to T.B., R.B. and K.-P.H.), National Institutes of Health U19 AI083025 (to K.-P.H.) and by the Fonds der chemischen Industrie (to S.F.).
PY - 2012/2/23
Y1 - 2012/2/23
N2 - 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.
AB - 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.
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U2 - 10.1038/nature10829
DO - 10.1038/nature10829
M3 - Article
C2 - 22358840
AN - SCOPUS:84857396073
SN - 0028-0836
VL - 482
SP - 501
EP - 506
JO - Nature
JF - Nature
IS - 7386
ER -