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Functionality of chimeric TssA proteins in the type VI secretion system reveals sheath docking specificity within their N-terminal domains

Author

Listed:
  • Selina Fecht

    (Imperial College London)

  • Patricia Paracuellos

    (Imperial College London)

  • Sujatha Subramoni

    (Nanyang Technological University)

  • Casandra Ai Zhu Tan

    (Nanyang Technological University)

  • Aravindan Ilangovan

    (Queen Mary University of London)

  • Tiago R. D. Costa

    (Imperial College London)

  • Alain Filloux

    (Imperial College London
    Nanyang Technological University)

Abstract

The genome of Pseudomonas aeruginosa encodes three type VI secretion systems, each comprising a dozen distinct proteins, which deliver toxins upon T6SS sheath contraction. The least conserved T6SS component, TssA, has variations in size which influence domain organisation and structure. Here we show that the TssA Nt1 domain interacts directly with the sheath in a specific manner, while the C-terminus is essential for oligomerisation. We built chimeric TssA proteins by swapping C-termini and showed that these can be functional even when made of domains from different TssA sub-groups. Functional specificity requires the Nt1 domain, while the origin of the C-terminal domain is more permissive for T6SS function. We identify two regions in short TssA proteins, loop and hairpin, that contribute to sheath binding. We propose a docking mechanism of TssA proteins with the sheath, and a model for how sheath assembly is coordinated by TssA proteins from this position.

Suggested Citation

  • Selina Fecht & Patricia Paracuellos & Sujatha Subramoni & Casandra Ai Zhu Tan & Aravindan Ilangovan & Tiago R. D. Costa & Alain Filloux, 2024. "Functionality of chimeric TssA proteins in the type VI secretion system reveals sheath docking specificity within their N-terminal domains," Nature Communications, Nature, vol. 15(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-48487-8
    DOI: 10.1038/s41467-024-48487-8
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    References listed on IDEAS

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    1. Samuel R. Dix & Hayley J. Owen & Ruyue Sun & Asma Ahmad & Sravanthi Shastri & Helena L. Spiewak & Daniel J. Mosby & Matthew J. Harris & Sarah L. Batters & Thomas A. Brooker & Svetomir B. Tzokov & Svet, 2018. "Structural insights into the function of type VI secretion system TssA subunits," Nature Communications, Nature, vol. 9(1), pages 1-16, December.
    2. Abdelrahim Zoued & Eric Durand & Yannick R. Brunet & Silvia Spinelli & Badreddine Douzi & Mathilde Guzzo & Nicolas Flaugnatti & Pierre Legrand & Laure Journet & Rémi Fronzes & Tâm Mignot & Christian C, 2016. "Priming and polymerization of a bacterial contractile tail structure," Nature, Nature, vol. 531(7592), pages 59-63, March.
    3. Maria Silvina Stietz & Xiaoye Liang & Hao Li & Xinran Zhang & Tao G. Dong, 2020. "TssA–TssM–TagA interaction modulates type VI secretion system sheath-tube assembly in Vibrio cholerae," Nature Communications, Nature, vol. 11(1), pages 1-11, December.
    4. Eric Durand & Van Son Nguyen & Abdelrahim Zoued & Laureen Logger & Gérard Péhau-Arnaudet & Marie-Stéphanie Aschtgen & Silvia Spinelli & Aline Desmyter & Benjamin Bardiaux & Annick Dujeancourt & Alain , 2015. "Biogenesis and structure of a type VI secretion membrane core complex," Nature, Nature, vol. 523(7562), pages 555-560, July.
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