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TssA–TssM–TagA interaction modulates type VI secretion system sheath-tube assembly in Vibrio cholerae

Author

Listed:
  • Maria Silvina Stietz

    (University of Calgary)

  • Xiaoye Liang

    (University of Calgary
    Shanghai Jiao Tong University)

  • Hao Li

    (Shanghai Jiao Tong University)

  • Xinran Zhang

    (University of Calgary)

  • Tao G. Dong

    (University of Calgary
    Shanghai Jiao Tong University)

Abstract

The type VI protein secretion system (T6SS) is a powerful needle-like machinery found in Gram-negative bacteria that can penetrate the cytosol of receiving cells in milliseconds by physical force. Anchored by its membrane-spanning complex (MC) and a baseplate (BP), the T6SS sheath-tube is assembled in a stepwise process primed by TssA and terminated by TagA. However, the molecular details of its assembly remain elusive. Here, we systematically examined the initiation and termination of contractile and non-contractile T6SS sheaths in MC-BP, tssA and tagA mutants by fluorescence microscopy. We observe long pole-to-pole sheath-tube structures in the non-contractile MC-BP defective mutants but not in the Hcp tube or VgrG spike mutants. Combining overexpression and genetic mutation data, we demonstrate complex effects of TssM, TssA and TagA interactions on T6SS sheath-tube dynamics. We also report promiscuous interactions of TagA with multiple T6SS components, similar to TssA. Our results demonstrate that priming of the T6SS sheath-tube assembly is not dependent on TssA, nor is the assembly termination dependent on the distal end TssA–TagA interaction, and highlight the tripartite control of TssA–TssM–TagA on sheath-tube initiation and termination.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:11:y:2020:i:1:d:10.1038_s41467-020-18807-9
    DOI: 10.1038/s41467-020-18807-9
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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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