Benzoate Decreases the Binding of cis , cis -Muconate to the BenM Regulator despite the Synergistic Effect of Both Compounds on Transcriptional Activation
Open Access
- 15 February 2004
- journal article
- Published by American Society for Microbiology in Journal of Bacteriology
- Vol. 186 (4) , 1200-1204
- https://doi.org/10.1128/jb.186.4.1200-1204.2004
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.Keywords
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