Two antagonistic response regulators control Pseudomonas aeruginosa polarization during mechanotaxis
Autor: | Marco J Kühn, Henriette Macmillan, Lorenzo Talà, Yuki Inclan, Ramiro Patino, Xavier Pierrat, Zainebe Al‐Mayyah, Joanne N Engel, Alexandre Persat |
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Rok vydání: | 2023 |
Předmět: |
General Immunology and Microbiology
General Neuroscience response regulators localization General Biochemistry Genetics and Molecular Biology cell polarity iv pili twitching motility chp chemosensory system frequency myxococcus-xanthus mechanosensing reversal chemotaxis genes Molecular Biology type iv pili complex |
Zdroj: | The EMBO Journal. 42 |
ISSN: | 1460-2075 0261-4189 |
DOI: | 10.15252/embj.2022112165 |
Popis: | The opportunistic pathogen Pseudomonas aeruginosa adapts to solid surfaces to enhance virulence and infect its host. Type IV pili (T4P), long and thin filaments that power surface-specific twitching motility, allow single cells to sense surfaces and control their direction of movement. T4P distribution is polarized to the sensing pole by the chemotaxis-like Chp system via a local positive feedback loop. However, how the initial spatially resolved mechanical signal is translated into T4P polarity is incompletely understood. Here, we demonstrate that the two Chp response regulators PilG and PilH enable dynamic cell polarization by antagonistically regulating T4P extension. By precisely quantifying the localization of fluorescent protein fusions, we show that phosphorylation of PilG by the histidine kinase ChpA controls PilG polarization. Although PilH is not strictly required for twitching reversals, it becomes activated upon phosphorylation and breaks the local positive feedback mechanism established by PilG, allowing forward-twitching cells to reverse. Chp thus uses a main output response regulator, PilG, to resolve mechanical signals in space and employs a second regulator, PilH, to break and respond when the signal changes. By identifying the molecular functions of two response regulators that dynamically control cell polarization, our work provides a rationale for the diversity of architectures often found in non-canonical chemotaxis systems. |
Databáze: | OpenAIRE |
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