Raw data for the role of acetyl phosphate in bypassing the cell membrane electrical potential sensor LytS

Data 1Autophosphorylation of LytS.Quantification of phosphorylated LytS bands by NIH Image J. Average of two trials. Data 2Phosphorylation of LytR by acetyl phosphate.Quantification of phosphorylated LytR bands by NIH ImageJ. Data 3Phosphorylation of LytR-N by acetyl phosphate.Quantification of phosphorylated LytR-N bands by NIH ImageJ. Data 4Quantification of LytR bands in native-PAGEs (Figure 6A and B) by NIH Image J. LytR protein was phosphorylated by acetyl phosphate and its dephosphorylation by LytS was monitored by native-PAGE, whereby the phosphorylated dimer LytR becomes monomer after dephosphorylation. The column “corrected” represents the data after correcting for background signal at 0 min, and considering the band labeled “Monomer”, in the absence of LytS and ATP, as 100% unphosphorylated LytR.