%0 Generic %A Patel, Kevin %A Golemi-Kotra, Dasantila %D 2016 %T Raw data for the role of acetyl phosphate in bypassing the cell membrane electrical potential sensor LytS %U https://f1000.figshare.com/articles/dataset/Raw_data_for_the_role_of_acetyl_phosphate_in_bypassing_the_cell_membrane_electrical_potential_sensor_LytS/3159043 %R 10.6084/m9.figshare.3159043.v1 %2 https://f1000.figshare.com/ndownloader/files/4920580 %2 https://f1000.figshare.com/ndownloader/files/4920583 %2 https://f1000.figshare.com/ndownloader/files/4920586 %2 https://f1000.figshare.com/ndownloader/files/4920589 %K LytSR %K histidine kinases %K response regulator proteins %K phosphotransfer %K Staphylococcus aureus %K Cell Biology %X

Data 1
Autophosphorylation of LytS.
Quantification of phosphorylated LytS bands by NIH Image J. Average of two trials.

Data 2
Phosphorylation of LytR by acetyl phosphate.
Quantification of phosphorylated LytR bands by NIH ImageJ.

Data 3
Phosphorylation of LytR-N by acetyl phosphate.
Quantification of phosphorylated LytR-N bands by NIH ImageJ.

Data 4
Quantification 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.

%I f1000research.com