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Structural insights into the function of type VI secretion system TssA subunits

Author

Listed:
  • Samuel R. Dix

    (University of Sheffield)

  • Hayley J. Owen

    (University of Sheffield)

  • Ruyue Sun

    (University of Sheffield Medical School)

  • Asma Ahmad

    (University of Sheffield Medical School)

  • Sravanthi Shastri

    (University of Sheffield Medical School)

  • Helena L. Spiewak

    (University of Sheffield Medical School
    Institute of Genetic Medicine, International Centre for Life)

  • Daniel J. Mosby

    (University of Sheffield Medical School)

  • Matthew J. Harris

    (University of Sheffield
    King’s College London, Britannia House)

  • Sarah L. Batters

    (University of Sheffield Medical School)

  • Thomas A. Brooker

    (University of Sheffield Medical School)

  • Svetomir B. Tzokov

    (University of Sheffield)

  • Svetlana E. Sedelnikova

    (University of Sheffield)

  • Patrick J. Baker

    (University of Sheffield)

  • Per A. Bullough

    (University of Sheffield)

  • David W. Rice

    (University of Sheffield)

  • Mark S. Thomas

    (University of Sheffield Medical School)

Abstract

The type VI secretion system (T6SS) is a multi-protein complex that injects bacterial effector proteins into target cells. It is composed of a cell membrane complex anchored to a contractile bacteriophage tail-like apparatus consisting of a sharpened tube that is ejected by the contraction of a sheath against a baseplate. We present structural and biochemical studies on TssA subunits from two different T6SSs that reveal radically different quaternary structures in comparison to the dodecameric E. coli TssA that arise from differences in their C-terminal sequences. Despite this, the different TssAs retain equivalent interactions with other components of the complex and position their highly conserved N-terminal ImpA_N domain at the same radius from the centre of the sheath as a result of their distinct domain architectures, which includes additional spacer domains and highly mobile interdomain linkers. Together, these variations allow these distinct TssAs to perform a similar function in the complex.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:9:y:2018:i:1:d:10.1038_s41467-018-07247-1
    DOI: 10.1038/s41467-018-07247-1
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    Cited by:

    1. 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.

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