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Previous studies have shown that the clcABD operon is under the transcriptional control of the LysR-type activator ClcR. In this study, the conditions leading to its aggregation were avoided and ClcR was purified and confirmed by amino-terminal sequencing. Gel filtration indicated that ClcR exists as a dimer in solution. The DNase I footprint of ClcR was determined. The binding properties of ClcR and the catechol operon regulator, CatR, were compared.

Purification of the LysR family regulator, ClcR, and its interaction with the Pseudomonas putida clcABD chlorocatechol operon promoter