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      Quorum sensing in Vibrio fischeri: probing autoinducer-LuxR interactions with autoinducer analogs.

      Journal of Bacteriology

      4-Butyrolactone, analogs & derivatives, metabolism, Bacterial Proteins, genetics, Binding, Competitive, Cell Communication, Escherichia coli, Gene Expression Regulation, Bacterial, Luminescent Measurements, Recombinant Proteins, Repressor Proteins, Trans-Activators, Transcription, Genetic, Vibrio

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          The Vibrio fischeri luminescence genes are activated by the transcription factor LuxR in combination with a diffusible signal compound, N-(3-oxohexanoyl) homoserine lactone, termed the autoinducer. We have synthesized a set of autoinducer analogs. Many analogs with alterations in the acyl side chain showed evidence of binding to LuxR. Some appeared to bind with an affinity similar to that of the autoinducer, but none showed a higher affinity, and many did not bind as tightly as the autoinducer. For the most part, compounds with substitutions in the homoserine lactone ring did not show evidence of binding to LuxR. The exceptions were compounds with a homocysteine thiolactone ring in place of the homoserine lactone ring. Many but not all of the analogs showing evidence of LuxR binding had some ability to activate the luminescence genes. None were as active as the autoinducer. While most showed little ability to induce luminescence, a few analogs with rather conservative substitutions had appreciable activity. Under the conditions we employed, some of the analogs showing little or no ability to induce luminescence were inhibitors of the autoinducer.

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