Publication Date:
2012-02-24
Description:
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.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Becker, Thomas -- Franckenberg, Sibylle -- Wickles, Stephan -- Shoemaker, Christopher J -- Anger, Andreas M -- Armache, Jean-Paul -- Sieber, Heidemarie -- Ungewickell, Charlotte -- Berninghausen, Otto -- Daberkow, Ingo -- Karcher, Annette -- Thomm, Michael -- Hopfner, Karl-Peter -- Green, Rachel -- Beckmann, Roland -- U19 AI083025/AI/NIAID NIH HHS/ -- Howard Hughes Medical Institute/ -- England -- Nature. 2012 Feb 22;482(7386):501-6. doi: 10.1038/nature10829.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Gene Center and Center for integrated Protein Science Munich, Department of Biochemistry, University of Munich, Feodor-Lynen-Strasse 25, 81377 Munich, Germany. becker@lmb.uni-muenchen.de〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/22358840" target="_blank"〉PubMed〈/a〉
Keywords:
ATP-Binding Cassette Transporters/chemistry/metabolism
;
Cell Cycle Proteins/chemistry/metabolism
;
Cryoelectron Microscopy
;
Endoribonucleases/chemistry/metabolism
;
*Evolution, Molecular
;
Iron-Sulfur Proteins/chemistry/metabolism
;
Models, Molecular
;
Movement
;
Multiprotein Complexes/chemistry/metabolism
;
Nuclear Proteins/chemistry/metabolism
;
Peptide Termination Factors/chemistry/metabolism
;
Protein Binding
;
Protein Stability
;
Protein Structure, Tertiary
;
Pyrococcus furiosus/*chemistry/metabolism
;
Ribosomes/*chemistry/*metabolism/ultrastructure
;
Saccharomyces cerevisiae/*chemistry/metabolism
;
Saccharomyces cerevisiae Proteins/chemistry/metabolism
Print ISSN:
0028-0836
Electronic ISSN:
1476-4687
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
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