Benzoate Decreases the Binding of cis , cis -Muconate to the BenM Regulator despite the Synergistic Effect of Both Compounds on Transcriptional Activation

Abstract
Fluorescence emission spectroscopy was used to investigate interactions between two effectors and BenM, a transcriptional regulator of benzoate catabolism. BenM had a higher affinity for cis , cis -muconate than for benzoate as the sole effector. However, the presence of benzoate increased the apparent dissociation constant (reduced the affinity) of the protein for cis , cis -muconate. Similar results were obtained with truncated BenM lacking the DNA-binding domain. High-level transcriptional activation may require that some monomers within a BenM tetramer bind benzoate and others bind cis , cis -muconate.

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