Journal
ACS CHEMICAL BIOLOGY
Volume 7, Issue 1, Pages 44-51Publisher
AMER CHEMICAL SOC
DOI: 10.1021/cb200445w
Keywords
Posttranslational modification (PTM); Phosphoproteomics; Histidine phosphorylation; Phosphoramidate; Histidine kinase; Two-component signaling system; Phosphohistidine analogue; Protein semisynthesis
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Funding
- National Institutes of Health [R01GM095880]
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM095880] Funding Source: NIH RePORTER
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This year (2012) marks the 50th anniversary of the discovery of protein histidine phosphorylation. Phosphorylation of histidine (pHis) is now widely recognized as being critical to signaling processes in prokaryotes and lower eukaryotes. However, the modification is also becoming more widely reported in mammalian cellular processes and implicated in certain human disease states such as cancer and inflammation. Nonetheless, much remains to be understood about the role and extent of the modification in mammalian cell biology. Studying the functional role of pHis in signaling, either in vitro or in vivo, has proven devilishly hard, largely due to the chemical instability of the modification. As a consequence, we are currently handicapped by a chronic lack of chemical and biochemical tools with which to study histidine phosphorylation. Here, we discuss the challenges associated with studying the chemical biology of pHis and review recent., progress that offers some hope that long-awaited biochemical reagents for studying this elusive posttranslational modification (PTM) might soon be available,
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