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Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins

Author

Listed:
  • Lars Ferbitz

    (Eidgenössische Technische Hochschule Hönggerberg (ETH Zürich))

  • Timm Maier

    (Eidgenössische Technische Hochschule Hönggerberg (ETH Zürich))

  • Holger Patzelt

    (Universität Heidelberg)

  • Bernd Bukau

    (Universität Heidelberg)

  • Elke Deuerling

    (Universität Heidelberg)

  • Nenad Ban

    (Eidgenössische Technische Hochschule Hönggerberg (ETH Zürich))

Abstract

During protein biosynthesis, nascent polypeptide chains that emerge from the ribosomal exit tunnel encounter ribosome-associated chaperones, which assist their folding to the native state1,2. Here we present a 2.7 Å crystal structure of Escherichia coli trigger factor, the best-characterized chaperone of this type, together with the structure of its ribosome-binding domain in complex with the Haloarcula marismortui large ribosomal subunit. Trigger factor adopts a unique conformation resembling a crouching dragon with separated domains forming the amino-terminal ribosome-binding ‘tail’, the peptidyl-prolyl isomerase ‘head’, the carboxy-terminal ‘arms’ and connecting regions building up the ‘back’. From its attachment point on the ribosome, trigger factor projects the extended domains over the exit of the ribosomal tunnel, creating a protected folding space where nascent polypeptides may be shielded from proteases and aggregation. This study sheds new light on our understanding of co-translational protein folding, and suggests an unexpected mechanism of action for ribosome-associated chaperones.

Suggested Citation

  • Lars Ferbitz & Timm Maier & Holger Patzelt & Bernd Bukau & Elke Deuerling & Nenad Ban, 2004. "Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins," Nature, Nature, vol. 431(7008), pages 590-596, September.
    • Handle: RePEc:nat:nature:v:431:y:2004:i:7008:d:10.1038_nature02899
    DOI: 10.1038/nature02899
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    Cited by:

    1. Simon M. Lauer & Maren Reepmeyer & Ole Berendes & Dorota Klepacki & Jakob Gasse & Sara Gabrielli & Helmut Grubmüller & Lars V. Bock & Andor Krizsan & Rainer Nikolay & Christian M. T. Spahn & Ralf Hoff, 2024. "Multimodal binding and inhibition of bacterial ribosomes by the antimicrobial peptides Api137 and Api88," Nature Communications, Nature, vol. 15(1), pages 1-19, December.
    2. Shivam Yadav & Martin Centola & Mathilda Glaesmann & Denys Pogoryelov & Roman Ladig & Mike Heilemann & L. C. Rai & Özkan Yildiz & Enrico Schleiff, 2022. "Cyclophilin anaCyp40 regulates photosystem assembly and phycobilisome association in a cyanobacterium," Nature Communications, Nature, vol. 13(1), pages 1-17, December.

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