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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.

journal of bacteriology

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

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