RRC ID 19103
Author 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.
Title Structural basis of highly conserved ribosome recycling in eukaryotes and archaea.
Journal Nature
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.
Volume 482(7386)
Pages 501-6
Published 2012-2-22
DOI 10.1038/nature10829
PII nature10829
PMID 22358840
PMC PMC6878762
MeSH ATP-Binding Cassette Transporters / chemistry ATP-Binding Cassette Transporters / metabolism Cell Cycle Proteins / chemistry Cell Cycle Proteins / metabolism Cryoelectron Microscopy Endoribonucleases / chemistry Endoribonucleases / metabolism Evolution, Molecular* Iron-Sulfur Proteins / chemistry Iron-Sulfur Proteins / metabolism Models, Molecular Movement Multiprotein Complexes / chemistry Multiprotein Complexes / metabolism Nuclear Proteins / chemistry Nuclear Proteins / metabolism Peptide Termination Factors / chemistry Peptide Termination Factors / metabolism Protein Binding Protein Stability Protein Structure, Tertiary Pyrococcus furiosus / chemistry* Pyrococcus furiosus / metabolism Ribosomes / chemistry* Ribosomes / metabolism* Ribosomes / ultrastructure Saccharomyces cerevisiae / chemistry* Saccharomyces cerevisiae / metabolism Saccharomyces cerevisiae Proteins / chemistry Saccharomyces cerevisiae Proteins / metabolism
IF 42.779
Times Cited 150
General Microbes JCM 12380