Patel, Kevin Golemi-Kotra, Dasantila Raw data for the role of acetyl phosphate in bypassing the cell membrane electrical potential sensor LytS <p>Data 1<br>Autophosphorylation of LytS.<br>Quantification of phosphorylated LytS bands by NIH Image J. Average of two trials.</p> <p>Data 2<br>Phosphorylation of LytR by acetyl phosphate.<br>Quantification of phosphorylated LytR bands by NIH ImageJ.</p> <p>Data 3<br>Phosphorylation of LytR-N by acetyl phosphate.<br>Quantification of phosphorylated LytR-N bands by NIH ImageJ.</p> <p>Data 4<br>Quantification of LytR bands in native-PAGEs (Figure 6A and B) by NIH Image J.</p> <p>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.</p> <p> </p> LytSR;histidine kinase;response regulator;phosphotransfer;Staphylococcus aureus;Cell Biology 2015-03-30
    https://f1000.figshare.com/articles/dataset/Raw_data_for_the_role_of_acetyl_phosphate_in_bypassing_the_cell_membrane_electrical_potential_sensor_LytS/1339843
10.6084/m9.figshare.1339843.v1