Open AccessSinorhizobium meliloti Fur-Like (Mur) Protein Binds a Fur Box-Like Sequence Present in the mntA Promoter in a Manganese-Responsive Manner
Author(s) -
Raúl Platero,
Vı́ctor de Lorenzo,
Beatríz Garat,
Elena Fabiano
Publication year - 2007
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.00686-07
Subject(s) - sinorhizobium meliloti , footprinting , manganese , biology , promoter , dna footprinting , gene , binding site , microbiology and biotechnology , dna , dna binding protein , binding protein , biochemistry , chemistry , transcription factor , gene expression , mutant , organic chemistry
InSinorhizobium 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 theS. meliloti mntA gene. We demonstrated that MurSm protein binds with high affinity to the promoter region ofmntA 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 themntA 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.