Despite the well-recognized biological importance of protein phosphorylation, non-conventional phosphorylations on histidine and arginine residues have evaded our attention and scrutiny for a long time. This lack of knowledge stems from the inherent chemical instability of phosphohistidine (pHis) and phosphoarginine (pArg), which makes the analysis of these phosphorylations notoriously challenging.<br/>Here we present our recent progress in developing fluorescent sensors to monitor the activity of the kinase and phosphatase that regulate these elusive forms of phosphorylation. Both synthetic and genetically encoded sensors have been successfully utilized for convenient real-time measurement of the target enzyme activities.

Chemical tools for studying non-conventional protein phosphorylations

ACS Spring 2022

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