Becker, Thomas and Franckenberg, Sibylle and Wickles, Stephan and Shoemaker, Christopher J. and Anger, Andreas M. and Armache, Jean-Paul and Sieber, Heidemarie and Ungewickell, Charlotte and Berninghausen, Otto and Daberkow, Ingo and Karcher, Annette and Thomm, Michael and Hopfner, Karl-Peter and Green, Rachel and Beckmann, Roland (2012) Structural basis of highly conserved ribosome recycling in eukaryotes and archaea. NATURE, 482 (7386). 501-U221. ISSN 0028-0836, 1476-4687
Full text not available from this repository. (Request a copy)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.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | MESSENGER-RNA DECAY; NO-GO DECAY; FREE PROTEIN-SYNTHESIS; X-RAY-STRUCTURE; ATP-BINDING; TRANSLATION TERMINATION; ELECTRON-MICROSCOPY; CRYSTAL-STRUCTURE; 80S RIBOSOME; THERMOCOCCUS-KODAKARAENSIS; |
| Subjects: | 500 Science > 570 Life sciences |
| Divisions: | Biology, Preclinical Medicine > Institut für Biochemie, Genetik und Mikrobiologie > Lehrstuhl für Mikrobiologie (Archaeenzentrum) > Prof. Dr. Michael Thomm |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 19 May 2020 07:07 |
| Last Modified: | 19 May 2020 07:07 |
| URI: | https://pred.uni-regensburg.de/id/eprint/19221 |
Actions (login required)
 |
View Item |
