@article{Fecht:2024:10.1038/s41467-024-48487-8,
author = {Fecht, S and Paracuellos, P and Subramoni, S and Tan, CAZ and Ilangovan, A and Costa, TRD and Filloux, A},
doi = {10.1038/s41467-024-48487-8},
journal = {Nature Communications},
title = {Functionality of chimeric TssA proteins in the type VI secretion system reveals sheath docking specificity within their N-terminal domains},
url = {http://dx.doi.org/10.1038/s41467-024-48487-8},
volume = {15},
year = {2024}
}

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TY  - JOUR
AB  - 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.
AU  - Fecht,S
AU  - Paracuellos,P
AU  - Subramoni,S
AU  - Tan,CAZ
AU  - Ilangovan,A
AU  - Costa,TRD
AU  - Filloux,A
DO  - 10.1038/s41467-024-48487-8
PY  - 2024///
SN  - 2041-1723
TI  - Functionality of chimeric TssA proteins in the type VI secretion system reveals sheath docking specificity within their N-terminal domains
T2  - Nature Communications
UR  - http://dx.doi.org/10.1038/s41467-024-48487-8
UR  - https://www.nature.com/articles/s41467-024-48487-8
UR  - http://hdl.handle.net/10044/1/111721
VL  - 15
ER  - 

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