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Structure of the signal recognition particle interacting with the elongation-arrested ribosome

Author

Listed:
  • Mario Halic

    (University Medical School, Humboldt University of Berlin)

  • Thomas Becker

    (University Medical School, Humboldt University of Berlin)

  • Martin R. Pool

    (University of Manchester, School of Biological Sciences)

  • Christian M. T. Spahn

    (University Medical School, Humboldt University of Berlin)

  • Robert A. Grassucci

    (Wadsworth Center, Empire State Plaza
    State University of New York at Albany)

  • Joachim Frank

    (Wadsworth Center, Empire State Plaza
    State University of New York at Albany)

  • Roland Beckmann

    (University Medical School, Humboldt University of Berlin)

Abstract

Cotranslational translocation of proteins across or into membranes is a vital process in all kingdoms of life. It requires that the translating ribosome be targeted to the membrane by the signal recognition particle (SRP), an evolutionarily conserved ribonucleoprotein particle. SRP recognizes signal sequences of nascent protein chains emerging from the ribosome. Subsequent binding of SRP leads to a pause in peptide elongation and to the ribosome docking to the membrane-bound SRP receptor. Here we present the structure of a targeting complex consisting of mammalian SRP bound to an active 80S ribosome carrying a signal sequence. This structure, solved to 12 Å by cryo-electron microscopy, enables us to generate a molecular model of SRP in its functional conformation. The model shows how the S domain of SRP contacts the large ribosomal subunit at the nascent chain exit site to bind the signal sequence, and that the Alu domain reaches into the elongation-factor-binding site of the ribosome, explaining its elongation arrest activity.

Suggested Citation

  • Mario Halic & Thomas Becker & Martin R. Pool & Christian M. T. Spahn & Robert A. Grassucci & Joachim Frank & Roland Beckmann, 2004. "Structure of the signal recognition particle interacting with the elongation-arrested ribosome," Nature, Nature, vol. 427(6977), pages 808-814, February.
    • Handle: RePEc:nat:nature:v:427:y:2004:i:6977:d:10.1038_nature02342
    DOI: 10.1038/nature02342
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    Cited by:

    1. Laura Czech & Christopher-Nils Mais & Hanna Kratzat & Pinku Sarmah & Pietro Giammarinaro & Sven-Andreas Freibert & Hanna Folke Esser & Joanna Musial & Otto Berninghausen & Wieland Steinchen & Roland B, 2022. "Inhibition of SRP-dependent protein secretion by the bacterial alarmone (p)ppGpp," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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