期刊
JOURNAL OF BACTERIOLOGY
卷 186, 期 4, 页码 1200-1204出版社
AMER SOC MICROBIOLOGY
DOI: 10.1128/JB.186.4.1200-1204.2004
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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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