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[…]

Using RIME for analysis of protein complex

The application of mass spectrometry for the analysis of protein complexes can be used in parallel with chromatin immunoprecipitation–sequencing experiments to provide information on both the cistrome and interactome for a given protein. Hisham Mohammed and colleagues developed the Rapid Immunoprecipitation Mass spectrometry of Endogenous protein (RIME) approach, a rapid and robust method to study chromatin and[…]