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Structure paper

TitleStructural basis of highly conserved ribosome recycling in eukaryotes and archaea.
Journal, issue, pagesNature, Vol. 482, Issue 7386, Page 501-506, Year 2012
Publish dateFeb 22, 2012
AuthorsThomas Becker / Sibylle Franckenberg / Stephan Wickles / Christopher J Shoemaker / Andreas M Anger / Jean-Paul Armache / Heidemarie Sieber / Charlotte Ungewickell / Otto Berninghausen / Ingo Daberkow / Annette Karcher / Michael Thomm / Karl-Peter Hopfner / Rachel Green / Roland Beckmann /
PubMed AbstractRibosome-driven protein biosynthesis is comprised of four phases: initiation, elongation, termination and recycling. In bacteria, ribosome recycling requires ribosome recycling factor and elongation ...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.
External linksNature / PubMed:22358840 / PubMed Central
MethodsEM (single particle)
Resolution6.6 - 7.2 Å
Structure data

EMDB-2008:
3D reconstruction of a translating yeast 80S ribosome in complex with Dom34p and Rli1p
Method: EM (single particle) / Resolution: 7.2 Å

2009

3j15

EMDB-2009: 3D reconstruction of an archaeal 70S ribosome in complex with aPelota and aABCE1
PDB-3j15: Model of ribosome-bound archaeal Pelota and ABCE1
Method: EM (single particle) / Resolution: 6.6 Å

2010

3j16

EMDB-2010: 3D reconstruction of a translating yeast 80S ribosome in complex with Dom34p and Rli1p
PDB-3j16: Models of ribosome-bound Dom34p and Rli1p and their ribosomal binding partners
Method: EM (single particle) / Resolution: 7.2 Å

Chemicals

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM / Adenosine diphosphate

ChemComp-SF4:
IRON/SULFUR CLUSTER / Iron–sulfur cluster

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM / Adenosine triphosphate

ChemComp-HOH:
WATER / Water

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • pyrococcus furiosus (archaea)
  • thermococcus kodakarensis (archaea)
KeywordsTRANSLATION/TRANSPORT PROTEIN / ribosome recycling / ribosome / archaea / TRANSLATION-TRANSPORT PROTEIN complex / translation / eukarya

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