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Towards the application of Tc toxins as a universal protein translocation system

Author

Listed:
  • Daniel Roderer

    (Max Planck Institute of Molecular Physiology)

  • Evelyn Schubert

    (Max Planck Institute of Molecular Physiology)

  • Oleg Sitsel

    (Max Planck Institute of Molecular Physiology)

  • Stefan Raunser

    (Max Planck Institute of Molecular Physiology)

Abstract

Tc toxins are bacterial protein complexes that inject cytotoxic enzymes into target cells using a syringe-like mechanism. Tc toxins are composed of a membrane translocator and a cocoon that encapsulates a toxic enzyme. The toxic enzyme varies between Tc toxins from different species and is not conserved. Here, we investigate whether the toxic enzyme can be replaced by other small proteins of different origin and properties, namely Cdc42, herpes simplex virus ICP47, Arabidopsis thaliana iLOV, Escherichia coli DHFR, Ras-binding domain of CRAF kinase, and TEV protease. Using a combination of electron microscopy, X-ray crystallography and in vitro translocation assays, we demonstrate that it is possible to turn Tc toxins into customizable molecular syringes for delivering proteins of interest across membranes. We also infer the guidelines that protein cargos must obey in terms of size, charge, and fold in order to apply Tc toxins as a universal protein translocation system.

Suggested Citation

  • Daniel Roderer & Evelyn Schubert & Oleg Sitsel & Stefan Raunser, 2019. "Towards the application of Tc toxins as a universal protein translocation system," Nature Communications, Nature, vol. 10(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-13253-8
    DOI: 10.1038/s41467-019-13253-8
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    Cited by:

    1. Alexander Belyy & Florian Lindemann & Daniel Roderer & Johanna Funk & Benjamin Bardiaux & Jonas Protze & Peter Bieling & Hartmut Oschkinat & Stefan Raunser, 2022. "Mechanism of threonine ADP-ribosylation of F-actin by a Tc toxin," Nature Communications, Nature, vol. 13(1), pages 1-12, December.
    2. Alexander Belyy & Philipp Heilen & Philine Hagel & Oliver Hofnagel & Stefan Raunser, 2023. "Structure and activation mechanism of the Makes caterpillars floppy 1 toxin," Nature Communications, Nature, vol. 14(1), pages 1-11, December.
    3. Shiheng Liu & Xian Xia & Eric Calvo & Z. Hong Zhou, 2023. "Native structure of mosquito salivary protein uncovers domains relevant to pathogen transmission," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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