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Applied and Environmental Microbiology, August 2007, p. 4832-4838, Vol. 73, No. 15
0099-2240/07/$08.00+0 doi:10.1128/AEM.00686-07
Copyright © 2007, American Society for Microbiology. All Rights Reserved.

Laboratorio de Ecología Microbiana, Instituto de Investigaciones Biológicas Clemente Estable, MEC, Unidad Asociada a la Facultad de Ciencias, Av. Italia 3318, Montevideo 11600, Uruguay,1 Centro Nacional de Biotecnología, CSIC, Campus de Cantoblanco, 28049 Madrid, Spain,2 Laboratorio de Interacciones Moleculares, Facultad de Ciencias, Iguá 4225, Montevideo 11400, Uruguay3
Received 26 March 2007/ Accepted 4 June 2007
In Sinorhizobium meliloti, the MurSm protein, a homologue of the ferric uptake regulator (Fur), mediates manganese-dependent regulation of the MntABCD manganese uptake system. In this study, we analyzed MurSm binding to the promoter region of the S. meliloti mntA gene. We demonstrated that MurSm protein binds with high affinity to the promoter region of mntA gene in a manganese-responsive manner. Moreover, the results presented here indicate that two monomers, or one dimer, of MurSm binds the DNA. The binding region was identified by DNase I footprinting analysis and covers a region of about 30 bp long that contains a palindromic sequence. The MurSm binding site, present in the mntA promoter region, is similar to a Fur box; however, manganese-activated MurSm binds a canonical Fur box with very low affinity. Furthermore, the data obtained indicate that MurSm responds to physiological concentrations of manganese.
Published ahead of print on 8 June 2007.
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