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

Selina Fecht, Patricia Paracuellos, Sujatha Subramoni, Casandra Ai Zhu Tan, Aravindan Ilangovan, Tiago R. D. Costa and Alain Filloux ()
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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

Nature Communications, 2024, vol. 15, issue 1, 1-13

Abstract: 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.

Date: 2024
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DOI: 10.1038/s41467-024-48487-8

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