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

For decades, major difficulties in analyzing histidine phosphorylation have limited the study of phosphohistidine signaling. Here researchers report a method revealing widespread and abundant protein histidine phosphorylation in Escherichia coli. They generated an extensive E. coli phosphoproteome data set, in which a remarkably high percentage  of phosphorylation sites are phosphohistidine sites. This resource should help enable a better understanding of the biological function of histidine phosphorylation. The Bioruptor Plus was used to prepare samples prior to mass spec analysis — sonication with the Bioruptor has been shown to allow detection of far more peptides than with heat treatment alone.

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