Journal
CELL
Volume 134, Issue 3, Pages 461-473Publisher
CELL PRESS
DOI: 10.1016/j.cell.2008.06.023
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Funding
- Howard Hughes Medical Institute, National Institutes of Health (NIH) [5R01GM065859]
- National Science Foundation [MCB-0343821]
- NIH [5R01 AI 054442, GM787552]
- National Cancer Institute's Initiative for Chemical Genetics, NIH, [N01-CO-12400]
- Broad Institute of Harvard
- MIT
- Department of Health and Human Service
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Quorum sensing, a process of bacterial cell-cell communication, relies on production, detection, and response to autoinducer signaling molecules. LuxN, a nine-transmembrane domain protein from Vibrio harveyi, is the founding example of membrane-bound receptors for acyl-homoserine lactone (AHL) autoinducers. We used mutagenesis and suppressor analyses to identify the AHL-binding domain of LuxN and discovered LuxN mutants that confer both decreased and increased AHL sensitivity. Our analysis of dose-response curves of multiple LuxN mutants pins these inverse phenotypes on quantifiable opposing shifts in the free-energy bias of LuxN for occupying its kinase and phosphatase states. To understand receptor activation and to characterize the pathway signaling parameters, we exploited a strong LuxN antagonist, one of fifteen small-molecule antagonists we identified. We find that quorum-sensing-mediated communication can be manipulated positively and negatively to control bacterial behavior and, more broadly, that signaling parameters can be deduced from in vivo data.
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