Benzoate Decreases the Binding of Cis,cis-muconate to the BenM Regulator Despite the Synergistic Effect of Both Compounds on Transcriptional Activation

Overview

Journal J Bacteriol

Publisher American Society for Microbiology

Specialty Microbiology

Date 2004 Feb 6

PMID 14762017

Citations 12

Authors

Todd J Clark

Robert S Phillips

Becky M Bundy

Cory Momany

Ellen L Neidle

Affiliations

Soon will be listed here.

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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