title: Structural basis of highly conserved ribosome recycling in eukaryotes and archaea.
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.
authors.affiliation: 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
authors.forename: Thomas
authors.initials: T
authors.lastname: Becker
authors.forename: Sibylle
authors.initials: S
authors.lastname: Franckenberg
authors.forename: Stephan
authors.initials: S
authors.lastname: Wickles
authors.forename: Christopher J
authors.initials: CJ
authors.lastname: Shoemaker
authors.forename: Andreas M
authors.initials: AM
authors.lastname: Anger
authors.forename: Jean-Paul
authors.initials: JP
authors.lastname: Armache
authors.forename: Heidemarie
authors.initials: H
authors.lastname: Sieber
authors.forename: Charlotte
authors.initials: C
authors.lastname: Ungewickell
authors.forename: Otto
authors.initials: O
authors.lastname: Berninghausen
authors.forename: Ingo
authors.initials: I
authors.lastname: Daberkow
authors.forename: Annette
authors.initials: A
authors.lastname: Karcher
authors.forename: Michael
authors.initials: M
authors.lastname: Thomm
authors.forename: Karl-Peter
authors.initials: KP
authors.lastname: Hopfner
authors.forename: Rachel
authors.initials: R
authors.lastname: Green
authors.forename: Roland
authors.initials: R
authors.lastname: Beckmann
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry / Q000378:metabolism; D018797:Cell Cycle Proteins / Q000737:chemistry / Q000378:metabolism; D020285:Cryoelectron Microscopy; D004722:Endoribonucleases / Q000737:chemistry / Q000378:metabolism; D019143:Evolution, Molecular; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism; D008958:Models, Molecular; D009068:Movement; D046912:Multiprotein Complexes / Q000737:chemistry / Q000378:metabolism; D009687:Nuclear Proteins / Q000737:chemistry / Q000378:metabolism; D010454:Peptide Termination Factors / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding; D055550:Protein Stability; D017434:Protein Structure, Tertiary; D020027:Pyrococcus furiosus / Q000737:chemistry* / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D012441:Saccharomyces cerevisiae / Q000737:chemistry* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism
chemical_list: D018528:ATP-Binding Cassette Transporters; D018797:Cell Cycle Proteins; D007506:Iron-Sulfur Proteins; D046912:Multiprotein Complexes; D009687:Nuclear Proteins; D010454:Peptide Termination Factors; C492990:RLI1 protein, S cerevisiae; D029701:Saccharomyces cerevisiae Proteins; C112808:Dom34 protein, S cerevisiae; D004722:Endoribonucleases