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Structural basis of highly conserved ribosome recycling in eukaryotes and archaea

Author

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  • Thomas Becker

    (Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany)

  • Sibylle Franckenberg

    (Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany)

  • Stephan Wickles

    (Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany)

  • Christopher J. Shoemaker

    (Howard Hughes Medical Institute, Johns Hopkins University School of Medicine)

  • Andreas M. Anger

    (Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany)

  • Jean-Paul Armache

    (Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany)

  • Heidemarie Sieber

    (Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany)

  • Charlotte Ungewickell

    (Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany)

  • Otto Berninghausen

    (Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany)

  • Ingo Daberkow

    (Tietz Video and Image Processing Systems GmbH, Eremitenweg 1)

  • Annette Karcher

    (Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany
    Rainer-Maria-Rilke-Gymnasium Icking)

  • Michael Thomm

    (NWF III/Biology and Preclinical Medicine, University of Regensburg, Universitätsstraße 31, 93053 Regensburg, Germany)

  • Karl-Peter Hopfner

    (Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany)

  • Rachel Green

    (Howard Hughes Medical Institute, Johns Hopkins University School of Medicine)

  • Roland Beckmann

    (Gene Center and Center for integrated Protein Science Munich (CiPSM), University of Munich, Feodor-Lynen-Straße 25, 81377 Munich, Germany)

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.

Suggested Citation

  • Thomas Becker & Sibylle Franckenberg & Stephan Wickles & Christopher J. Shoemaker & Andreas M. Anger & Jean-Paul Armache & Heidemarie Sieber & Charlotte Ungewickell & Otto Berninghausen & Ingo Daberko, 2012. "Structural basis of highly conserved ribosome recycling in eukaryotes and archaea," Nature, Nature, vol. 482(7386), pages 501-506, February.
    • Handle: RePEc:nat:nature:v:482:y:2012:i:7386:d:10.1038_nature10829
    DOI: 10.1038/nature10829
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    Cited by:

    1. Momoko Narita & Timo Denk & Yoshitaka Matsuo & Takato Sugiyama & Chisato Kikuguchi & Sota Ito & Nichika Sato & Toru Suzuki & Satoshi Hashimoto & Iva Machová & Petr Tesina & Roland Beckmann & Toshifumi, 2022. "A distinct mammalian disome collision interface harbors K63-linked polyubiquitination of uS10 to trigger hRQT-mediated subunit dissociation," Nature Communications, Nature, vol. 13(1), pages 1-16, December.
    2. Ken Ikeuchi & Nives Ivic & Robert Buschauer & Jingdong Cheng & Thomas Fröhlich & Yoshitaka Matsuo & Otto Berninghausen & Toshifumi Inada & Thomas Becker & Roland Beckmann, 2023. "Molecular basis for recognition and deubiquitination of 40S ribosomes by Otu2," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    3. Antonios Apostolopoulos & Naohiro Kawamoto & Siu Yu A. Chow & Hitomi Tsuiji & Yoshiho Ikeuchi & Yuichi Shichino & Shintaro Iwasaki, 2024. "dCas13-mediated translational repression for accurate gene silencing in mammalian cells," Nature Communications, Nature, vol. 15(1), pages 1-18, December.

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