Benzoate decreases the binding of cis,cis-muconate to the BenM regulator despite the synergistic effect of both compounds on transcriptional activation.
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.
Clark
Todd J
TJ
Departments of Microbiology. Chemistry, and Pharmaceutical. Biomedical Sciences, University of Georgia, Athens, Georgia 30602.
Phillips
Robert S
RS
Bundy
Becky M
BM
Momany
Cory
C
Neidle
Ellen L
EL
D001426:Bacterial Proteins; D001565:Benzoates / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D004247:DNA / Q000378:metabolism; D013011:Sorbic Acid / Q000031:analogs & derivatives* / Q000737:chemistry / Q000378:metabolism*; D013050:Spectrometry, Fluorescence; D014157:Transcription Factors / Q000737:chemistry / Q000378:metabolism*; D015533:Transcriptional Activation
D001426:Bacterial Proteins; C112178:BenM protein, Acinetobacter; D001565:Benzoates; D014157:Transcription Factors; C005939:muconic acid; D004247:DNA; D013011:Sorbic Acid