Widespread bacterial protein histidine phosphorylation revealed by mass spectrometry-based proteomics

Clement M Potel, Miao-Hsia Lin, Albert J R Heck, Simone Lemeer

For decades, major difficulties in analyzing histidine phosphorylation have limited the study of phosphohistidine signaling. Here we report a method revealing widespread and abundant protein histidine phosphorylation in Escherichia coli. We generated an extensive E. coli phosphoproteome data set, in which a remarkably high percentage (∼10%) of phosphorylation sites are phosphohistidine sites. This resource should help enable a better understanding of the biological function of histidine phosphorylation.

Widespread bacterial protein histidine phosphorylation revealed by mass spectrometry-based proteomics

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