Abstract
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.
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