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

Nat Methods. 2018 Mar;15(3):187-190. doi: 10.1038/nmeth.4580. Epub 2018 Jan 29.


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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / metabolism*
  • Histidine / metabolism*
  • Mass Spectrometry / methods*
  • Phosphorylation
  • Proteomics / methods*


  • Escherichia coli Proteins
  • Histidine