Widespread bacterial protein histidine phosphorylation revealed by mass spectrometry-based proteomics.
basic_science · Level V
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- Record sourced from PubMed, PMID 29377012.
- Also identified by DOI 10.1038/nmeth.4580.
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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.
Medical subject headings
- Escherichia coli
- Escherichia coli Proteins
- Histidine
- Mass Spectrometry
- Proteomics