dc.contributor.author | Fecht, S | en_US |
dc.contributor.author | Paracuellos, P | en_US |
dc.contributor.author | Subramoni, S | en_US |
dc.contributor.author | Tan, CAZ | en_US |
dc.contributor.author | Ilangovan, A | en_US |
dc.contributor.author | Costa, TRD | en_US |
dc.contributor.author | Filloux, A | en_US |
dc.date.accessioned | 2024-06-20T08:39:55Z | |
dc.date.available | 2024-05-01 | en_US |
dc.date.issued | 2024-05-20 | en_US |
dc.identifier.uri | https://qmro.qmul.ac.uk/xmlui/handle/123456789/97542 | |
dc.description.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. | en_US |
dc.format.extent | 4283 - ? | en_US |
dc.language | eng | en_US |
dc.relation.ispartof | Nat Commun | en_US |
dc.rights | This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. | |
dc.subject | Type VI Secretion Systems | en_US |
dc.subject | Pseudomonas aeruginosa | en_US |
dc.subject | Bacterial Proteins | en_US |
dc.subject | Protein Domains | en_US |
dc.subject | Protein Binding | en_US |
dc.subject | Recombinant Fusion Proteins | en_US |
dc.title | Functionality of chimeric TssA proteins in the type VI secretion system reveals sheath docking specificity within their N-terminal domains. | en_US |
dc.type | Article | |
dc.rights.holder | © The Author(s) 2023 | |
dc.identifier.doi | 10.1038/s41467-024-48487-8 | en_US |
pubs.author-url | https://www.ncbi.nlm.nih.gov/pubmed/38769318 | en_US |
pubs.issue | 1 | en_US |
pubs.notes | Not known | en_US |
pubs.publication-status | Published online | en_US |
pubs.volume | 15 | en_US |
dcterms.dateAccepted | 2024-05-01 | en_US |
rioxxterms.funder | Default funder | en_US |
rioxxterms.identifier.project | Default project | en_US |
rioxxterms.funder.project | 2acae7f5-fd8c-4d20-af2e-447fb9664166 | en_US |