ArticleInternational journal of molecular sciences2013
Kinetic model for signal binding to the Quorum sensing regulator LasR.
Article in International journal of molecular sciences, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 15 citations in OpenAlex.
- Domain-Swapped LuxR-Type Quorum Sensing Receptors Reveal Divergent Ligand-Response Mechanisms among Homologues.Journal of the American Chemical Society · 2026Article
- An Experimentally Verified Mechanistic Model for Predicting Quorum Sensing-Based Switches.Microbial biotechnology · 2026Article
- Population-level bistability inmBio · 2025Article
- DyMMM-LEAPS: An ML-based framework for modulating evenness and stability in synthetic microbial communities.Biophysical journal · 2024Article
- Single-cell level LasR-mediated quorum sensing response of Pseudomonas aeruginosa to pulses of signal molecules.Scientific reports · 2024Article
- Bacteria Floc, but Do They Flock? Insights from Population Interaction Models of Quorum Sensing.mBio · 2019Article
- How fast is a collective bacterial state established?PloS one · 2017Article
- Using surface enhanced Raman scattering to analyze the interactions of protein receptors with bacterial quorum sensing modulators.ACS nano · 2015Article
- Microbial biofilm as a smart material.Sensors (Basel, Switzerland) · 2015Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
We propose a kinetic model for the activation of the las regulon in the opportunistic pathogen Pseudomonas aeruginosa. The model is based on in vitro data and accounts for the LasR dimerization and consecutive activation by binding of two OdDHL signal molecules. Experimentally, the production of the active LasR quorum-sensing regulator was studied in an Escherichia coli background as a function of signal molecule concentration. The functional activity of the regulator was monitored via a GFP reporter fusion to lasB expressed from the native lasB promoter. The new data shows that the active form of the LasR dimer binds two signal molecules cooperatively and that the timescale for reaching saturation is independent of the signal molecule concentration. This favors a picture where the dimerized regulator is protected against proteases and remains protected as it is activated through binding of two successive signal molecules. In absence of signal molecules, the dimerized regulator can dissociate and degrade through proteolytic turnover of the monomer. This resolves the apparent contradiction between our data and recent reports that the fully protected dimer is able to "degrade" when the induction of LasR ceases.
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