Clark Todd J, Phillips Robert S, Bundy Becky M, Momany Cory, Neidle Ellen L
Departments of Microbiology. Chemistry, and Pharmaceutical. Biomedical Sciences, University of Georgia, Athens, Georgia 30602.
J Bacteriol. 2004 Feb;186(4):1200-4. doi: 10.1128/JB.186.4.1200-1204.2004.
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.
荧光发射光谱法被用于研究两种效应物与苯甲酸酯分解代谢的转录调节因子BenM之间的相互作用。作为唯一的效应物,BenM对顺,顺-粘康酸的亲和力高于对苯甲酸酯的亲和力。然而,苯甲酸酯的存在增加了蛋白质对顺,顺-粘康酸的表观解离常数(降低了亲和力)。对于缺乏DNA结合结构域的截短型BenM也获得了类似的结果。高水平的转录激活可能要求BenM四聚体内的一些单体结合苯甲酸酯,而其他单体结合顺,顺-粘康酸。