csgBA is positively regulated by the global regulator CsgD
First , we show that unphosphorylated CsgD binds to the promoter regions of its target genes csgBA and adrA and stimulates their transcription in-vitro .
Results CsgD binds directly to adrA promoter regions In S. Typhimurium the expression of csgBA is positively regulated by the transcriptional regulator CsgD .
Results CsgD binds directly to the csgBA In S. Typhimurium the expression of adrA is positively regulated by the transcriptional regulator CsgD .
Results CsgD binds directly to the csgBA In S. Typhimurium the expression of csgBA is positively regulated by the transcriptional regulator CsgD .
Results CsgD binds directly to the csgBA In S. Typhimurium the expression of csgBA is positively regulated by the transcriptional regulator CsgD .
In order to demonstrate the direct binding of CsgD to the csgBA promoter regions we performed EMSA with purified CsgD-His6 tagged protein ( Fig .
In order to demonstrate the direct binding of CsgD to the csgBA promoter regions we performed electrophoretic-mobility-shift assays with purified CsgD-His6 tagged protein ( Fig .
Since CsgD is highly integrated into the c-di-GMP signalling network , we investigated whether c-di-GMP affects the binding of CsgD-His6 to the csgBA .
Pre-incubation of CsgD-His6 with 10 mM AcP led to a decreased binding of CsgD to the csgBA promoter fragments , compared with Fig. 5A .
Pre-incubation of CsgD-His6 with 10 mM AcP led to a decreased binding of CsgD to the csgBA promoter fragments , compared with CsgD alone .
Since the binding of CsgD to the csgBA is altered in the presence of the phosphodonor AcP , we investigated whether CsgD can be phosphorylated in-vitro .
However , we discovered that c-di-GMP , is not required for binding of CsgD to the csgBA promoters .
However , we discovered that an integral part of the regulatory network , is not required for binding of CsgD to the csgBA promoters .
CsgD directly binds to the csgBA upstream promoter region and positively regulates the expression of cellulose biosynthesis by activating expression of adrA , encoding a diguanylate cyclase .