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

AUTOR(ES)

Clark, Todd J.

FONTE

American Society for Microbiology

RESUMO

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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