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

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

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...

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Bibliographic Details
Main Authors: Fecht, Selina, Paracuellos, Patricia, Subramoni, Sujatha, Tan, Casandra Ai Zhu, Ilangovan, Aravindan, Costa, Tiago R. D., Filloux, Alain
Other Authors: School of Biological Sciences
Format: Journal Article
Language:English
Published: 2024
Subjects:
Medicine, Health and Life Sciences
Bacterial protein
Amino terminal sequence
Online Access:https://hdl.handle.net/10356/178817

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