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. 1999 Oct;8(10):2177–2185. doi: 10.1110/ps.8.10.2177

Protein histidine phosphorylation: increased stability of thiophosphohistidine.

M Lasker 1, C D Bui 1, P G Besant 1, K Sugawara 1, P Thai 1, G Medzihradszky 1, C W Turck 1
PMCID: PMC2144125  PMID: 10548064

Abstract

Posttranslational phosphorylation of proteins is an important event in many cellular processes. Whereas phosphoesters of serine, threonine and tyrosine have been extensively studied, only limited information is available for other amino acids modified by a phosphate group. The formation of phosphohistidine residues in proteins has been discovered in prokaryotic organisms as well as in eukaryotic cells. The ability to biochemically analyze phosphohistidine residues in proteins, however, is severely hampered by its extreme lability under acidic conditions. In our studies we have found that by replacing the phosphate linked to the histidine residue with a thiophosphate, a phosphohistidine derivative with increased stability is formed. This allows the analysis of phosphohistidine-containing proteins by established biochemical techniques and will greatly aid in the investigation of the role of this posttranslational modification in cellular processes.

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Selected References

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