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The multiple antibiotic resistance regulatory protein(MarR) binds to two promoter sites on the marO operator in Escherichia coli.Our study showed that more than one MarR dimer proteins bound to either of its two promoter sites(Site I and Site II),suggesting that MarR might form higher complexes than homodimers when bound to DNA inside E.coli cells.To further verify this hypothesis,we site-specifically incorporated a photocrosslinking probe at the interface between two MarR dimer proteins.Photolysis in living E.coli cells revealed a covalent linkage between the two interdimer subunits of MarR,suggesting that MarR forms dimer of dimers in vivo.
The multiple antibiotic resistance regulatory protein (MarR) binds to two promoter sites on the marO operator in Escherichia coli. Our study showed that more than one MarR dimer proteins bound to either of its two promoter sites (Site I and Site II), suggesting that MarR might form higher complexes than homodimers when bound to DNA inside E. coli cells. To further verify this hypothesis, we site-specifically incorporated a photocrosslinking probe at the interface between two MarR dimer proteins. Photolysis in living E. coli cells revealed a covalent linkage between the two interdimer subunits of MarR, suggesting that MarR forms dimer of dimers in vivo.