The effects of L-arginine on protein stability and DNA binding ability of SaeR, a transcription factor in Staphylococcus aureus

The SaeRS two-component system in Staphylococcus aureus controls the expression of a series of virulence factors, such as hemolysins, pmteases, and coagulase. The response regulator, SaeR, belongs to the OmpR family with an N-terminal regulatory domain and a C-terminal DNA binding domain. To improve the production and stability of the recombinant protein SaeR, L-arginine (L-Arg) was added to the purification buffers. L-Arg enhanced the solubility and stability of the recombinant protein SaeR. The thermal denaturation temperature of SaeR in 10 mM L-Arg buffer was significantly increased compared to the buffer without L-Arg. Microscale Thermophoresis (MST) analysis results showed that the SaeR protein could bind to the P1 promoter under both phosphorylated and non-phosphorylated status in buffer containing 10 mM L-Arg. These results illustrate an effective method to purify SaeR and other proteins.

Automated summary

The SaeRS two-component system in Staphylococcus aureus regulates the expression of virulence factors, and adding L-arginine to purification buffers can improve the stability and solubility of recombinant protein SaeR. The thermal denaturation temperature of SaeR is significantly increased in 10 mM L-Arg buffer, and MST analysis shows that SaeR can bind to the P1 promoter under different phosphorylation statuses in buffers containing L-Arg. These findings suggest an effective method for purifying SaeR and other proteins.