Fig. 5: Autophosphorylation of HK853 and phosphotransfer to RR468.
From: Revisiting the pH-gated conformational switch on the activities of HisKA-family histidine kinases
a Time course of HK853 autophosphorylation with [γ-32P] ATP at different pHs. b Stability of phosphorylated HK853 at acidic (5) and basic (8) pH. Phosphorylation was quantified by autoradiography, phosphorylation signals at t = 0 were set to 100% for each pH and phoshorylation were calculated accordingly. Values were plotted in a semi logarithmic scale over time, using a linear fit to calculate half-life times of HK853–P at each pH. c Time course of phosphotransfer from HK853 to RR468 at acidic (5) and basic (8) pH. Gels correspond to a representative experiment and quantification of three independent experiments are plotted. Error bars represent SD. Source data are provided as a Source Data file.
