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

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

Clement M Potel  1   2 , Miao-Hsia Lin  1   2 , Albert J R Heck  1   2 , Simone Lemeer  1   2
Affiliations

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

Clement M Potel et al. Nat Methods. 2018 Mar.

Abstract

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.

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References

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