Francis, Vanessa I, Waters, Elaine M, Finton-James, Sutharsan E, Gori, Andrea, Kadioglu, Aras
ORCID: 0000-0003-1137-6321, Brown, Alan R and Porter, Steven L
(2018)
Multiple communication mechanisms between sensor kinases are crucial for virulence in Pseudomonas aeruginosa
NATURE COMMUNICATIONS, 9 (1).
2219-.
ISSN 2041-1723, 2041-1723
Abstract
Bacteria and many non-metazoan Eukaryotes respond to stresses and threats using two-component systems (TCSs) comprising sensor kinases (SKs) and response regulators (RRs). Multikinase networks, where multiple SKs work together, detect and integrate different signals to control important lifestyle decisions such as sporulation and virulence. Here, we study interactions between two SKs from Pseudomonas aeruginosa, GacS and RetS, which control the switch between acute and chronic virulence. We demonstrate three mechanisms by which RetS attenuates GacS signalling: RetS takes phosphoryl groups from GacS-P; RetS has transmitter phosphatase activity against the receiver domain of GacS-P; and RetS inhibits GacS autophosphorylation. These mechanisms play important roles in vivo and during infection, and exemplify an unprecedented degree of signal processing by SKs that may be exploited in other multikinase networks.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | Animals, Mice, Inbred BALB C, Humans, Mice, Moths, Pseudomonas aeruginosa, Pseudomonas Infections, Disease Models, Animal, Phosphotransferases, Bacterial Proteins, Virulence Factors, Anti-Bacterial Agents, Virulence, Signal Transduction, Phosphorylation, Female, Protein Interaction Maps, Protein Domains |
| Depositing User: | Symplectic Admin |
| Date Deposited: | 11 Feb 2019 11:50 |
| Last Modified: | 23 May 2026 01:35 |
| DOI: | 10.1038/s41467-018-04640-8 |
| Open Access URL: | https://doi.org/10.1038/s41467-018-04640-8 |
| Related Websites: | |
| URI: | https://livrepository.liverpool.ac.uk/id/eprint/3032638 |
| Disclaimer: | The University of Liverpool is not responsible for content contained on other websites from links within repository metadata. Please contact us if you notice anything that appears incorrect or inappropriate. |
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