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

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

doi:10.1038/nmeth.4580

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.

Authors

Clement M Potel^{1

2}, Miao-Hsia Lin^{1

2}, Albert J R Heck^{1

2}, Simone Lemeer^{1

2}

Affiliations

¹ Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences, University of Utrecht, Utrecht, the Netherlands.
² Netherlands Proteomics Center, Utrecht, the Netherlands.

PMID: 29377012
DOI: 10.1038/nmeth.4580

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.

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*

Substances

Escherichia coli Proteins
Histidine