TAILIEUCHUNG - Báo cáo Y học: Phosphorylation and dephosphorylation of histidine residues in proteins Susanne Klumpp and Josef Krieglstein Abteilung Biochemie und Institut fu¨r Pharmakologie und

Protein phosphorylation is a key mechanism for intracellular signal transduction in both prokaryotic and eukaryotic cells. Vertebrate proteins are prevalently phosphorylated on side chains that contain a hydroxyl group, such as serine, threonine and tyrosine residues. In the past decade, however, an increasing number of examples of histidine phosphorylation has been described. Because acid treatment of phosphoproteins during purification and detection of phosphoamino acid analysis is routine, O-phosphomonoesters have been studied more often, and the existence of acid-labile phosphates has been largely overlooked | Eur. J. Biochem. 269 1067-1071 2002 FEBS 2002 MINIREVIEW Phosphorylation and dephosphorylation of histidine residues in proteins Susanne Klumpp and Josef Krieglstein Abteilung Biochemie und Institut fur Pharmakologie und Toxikologie Fachbereich Pharmazie Philipps-Universitat Marburg Germany Protein phosphorylation is a key mechanism for intracellular signal transduction in both prokaryotic and eukaryotic cells. Vertebrate proteins are prevalently phosphorylated on side chains that contain a hydroxyl group such as serine threonine and tyrosine residues. In the past decade however an increasing number of examples of histidine phosphorylation has been described. Because acid treatment of phosphoproteins during purification and detection of phosphoamino acid analysis is routine O-phosphomonoesters have been studied more often and the existence of acid-labile phosphates has been largely overlooked. The latter class of N-phosphoamidates may well be more widespread than is generally believed even though the O-phosphates remain the major class in terms of quantity and extent of distribution in proteins. Phosphohistidine currently is estimated to be 10- to 100-fold more abundant than phosphotyrosine but less abundant than phosphoserine Matthews . 1995 Pharmac. Ther. 67 323-350. . This minireview briefly summarizes the extensive knowledge of the key mechanisms and functions of phosphohistidine in bacteria. It also describes the still limited yet increasing data from homologs of the bacterial two-component system. Finally novel mechanisms of phosphorylation and dephosphorylation of histidine residues not related to the two-component system are described. Keywords signal transduction histidine kinase phosphatase two-component system. CHEMISTRY STABILITY AND DETECTION OF P H O S P H O H IS TI DI N E Whereas phosphorylation of serine threonine or tyrosine results in the formation of a phosphoester linkage phosphorylation of histidine residues occurs on nitrogen atoms .

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