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      Signal production and detection specificity in Vibrio CqsA/CqsS quorum-sensing systems

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          Summary

          Quorum sensing is a process of bacterial cell–cell communication that enables populations of cells to carry out behaviours in unison. Quorum sensing involves detection of the density-dependent accumulation of extracellular signal molecules called autoinducers that elicit population-wide changes in gene expression. In Vibrio species, CqsS is a membrane-bound histidine kinase that acts as the receptor for the CAI-1 autoinducer which is produced by the CqsA synthase. In Vibrio cholerae, CAI-1 is ( S)-3-hydroxytridecan-4-one. The C170 residue of V. cholerae CqsS specifies a preference for a ligand with a 10-carbon tail length. However, a phenylalanine is present at this position in Vibrio harveyi CqsS and other homologues, suggesting that a shorter CAI-1-like molecule functions as the signal. To investigate this, we purified the V. harveyi CqsS ligand, and determined that it is ( Z)-3-aminoundec-2-en-4-one (Ea-C8-CAI-1) carrying an 8-carbon tail. The V. harveyi CqsA/CqsS system is exquisitely selective for production and detection of this ligand, while the V. cholerae CqsA/CqsS counterparts show relaxed specificity in both production and detection. We isolated CqsS mutants in each species that display reversed specificity for ligands. Our analysis provides insight into how fidelity is maintained in signal transduction systems.

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          Molecular Cloning : A Laboratory Manual

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            Bacterial quorum-sensing network architectures.

            Quorum sensing is a cell-cell communication process in which bacteria use the production and detection of extracellular chemicals called autoinducers to monitor cell population density. Quorum sensing allows bacteria to synchronize the gene expression of the group, and thus act in unison. Here, we review the mechanisms involved in quorum sensing with a focus on the Vibrio harveyi and Vibrio cholerae quorum-sensing systems. We discuss the differences between these two quorum-sensing systems and the differences between them and other paradigmatic bacterial signal transduction systems. We argue that the Vibrio quorum-sensing systems are optimally designed to precisely translate extracellular autoinducer information into internal changes in gene expression. We describe how studies of the V. harveyi and V. cholerae quorum-sensing systems have revealed some of the fundamental mechanisms underpinning the evolution of collective behaviors.
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              Structural identification of a bacterial quorum-sensing signal containing boron.

              Cell-cell communication in bacteria is accomplished through the exchange of extracellular signalling molecules called autoinducers. This process, termed quorum sensing, allows bacterial populations to coordinate gene expression. Community cooperation probably enhances the effectiveness of processes such as bioluminescence, virulence factor expression, antibiotic production and biofilm development. Unlike other autoinducers, which are specific to a particular species of bacteria, a recently discovered autoinducer (AI-2) is produced by a large number of bacterial species. AI-2 has been proposed to serve as a 'universal' signal for inter-species communication. The chemical identity of AI-2 has, however, proved elusive. Here we present the crystal structure of an AI-2 sensor protein, LuxP, in a complex with autoinducer. The bound ligand is a furanosyl borate diester that bears no resemblance to previously characterized autoinducers. Our findings suggest that addition of naturally occurring borate to an AI-2 precursor generates active AI-2. Furthermore, they indicate a potential biological role for boron, an element required by a number of organisms but for unknown reasons.
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                Author and article information

                Journal
                Mol Microbiol
                Mol. Microbiol
                mmi
                Molecular Microbiology
                Blackwell Publishing Ltd (Oxford, UK )
                0950-382X
                1365-2958
                March 2011
                26 January 2011
                : 79
                : 6
                : 1407-1417
                Affiliations
                [1 ]Departments of Molecular Biology
                [2 ]Chemistry, Princeton University Princeton, NJ, USA
                [3 ]Lotus Separations LLC Princeton, NJ, USA
                [4 ]Howard Hughes Medical Institute Chevy Chase, MD, USA
                Author notes
                *For correspondence. E-mail bbassler@ 123456princeton.edu ; Tel. (+1) 609 258 2857; Fax (+1) 609 258 2957.
                Article
                10.1111/j.1365-2958.2011.07548.x
                3285556
                21219472
                70e7c4a5-01a7-4b96-a09f-385a2d55aa58
                © 2011 Blackwell Publishing Ltd

                Re-use of this article is permitted in accordance with the Creative Commons Deed, Attribution 2.5, which does not permit commercial exploitation.

                History
                : 05 January 2011
                Categories
                Research Articles

                Microbiology & Virology
                Microbiology & Virology

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