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Journal of Bacteriology, February 2004, p. 1200-1204, Vol. 186, No. 4
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.4.1200-1204.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

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

Todd J. Clark,1,{dagger} Robert S. Phillips,2 Becky M. Bundy,1,{ddagger} Cory Momany,3 and Ellen L. Neidle1*

Departments of Microbiology,1 Chemistry, and Pharmaceutical,2 Biomedical Sciences, University of Georgia, Athens, Georgia 306023

Received 9 April 2003/ Accepted 3 November 2003

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.

* Corresponding author. Mailing address: Department of Microbiology, University of Georgia, Athens, GA 30602-2605. Phone: (706) 542-2852. Fax: (706) 542-2674. E-mail: eneidle{at}uga.edu.

{dagger} Present address: Gastroenterology Research Unit, Mayo Clinic, Rochester, MN 55905.

{ddagger} Present address: Center for Tropical and Emerging Global Diseases, University of Georgia, Athens, GA 30602.

Journal of Bacteriology, February 2004, p. 1200-1204, Vol. 186, No. 4
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.4.1200-1204.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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