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

@article{Potel2018WidespreadBP,
  title={Widespread bacterial protein histidine phosphorylation revealed by mass spectrometry-based proteomics},
  author={Clement Potel and Miao-Hsia Lin and Albert J. R. Heck and Simone Lemeer},
  journal={Nature Methods},
  year={2018},
  volume={15},
  pages={187-190}
}
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… 

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