New Histone Kinases in Nuclei of Rat Tissues

Smtih, D L; Bruegger, Berndt B.; Halpern, Richard M.; Smith, Rhona

doi:10.1038/246103a0

Cited by 78 publications

(44 citation statements)

References 13 publications

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“…Phosphohistidine was originally detected in mammalian cells in mitochondria derived from bovine liver~Boyer et al, 1962! and nuclei from rat tissuẽ Smith et al, 1973!. It was also found that phosphorylation of a histidine on the cytoplasmic tail of P-selectin takes place following platelet activation with thrombin or collagen~Crovello et al, 1995!.…”

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confidence: 99%

Protein histidine phosphorylation: Increased stability of thiophosphohistidine

et al. 1999

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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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confidence: 99%

Protein histidine phosphorylation: Increased stability of thiophosphohistidine

et al. 1999

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“…However, almost all other studies in eukaryotes have focused on the phosphorylation of serine, threonine and tyrosine residues since partial acid hydrolysis, as used for conventional phosphoamino acid analysis, destroys the phosphoramidate bonds found in phosphohistidine, phospholysine or phosphoarginine [7]. Phosphoramidate bonds and protein kinases that phosphorylate arginine, histidine or lysine have been reported in eukaryotes [8][9][10][11][12][13][14][15][16][17][18][19][20][21][22][23][24][25] and reviewed recently [26]. Saccharomyces cerevisiae contains a kinase that transfers phosphate from ATP to histidine-75 in the protein, histone H4, in vitro [27].…”

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confidence: 99%

Protein histidine phosphatase activity in rat liver and spinach leaves

Matthews

MacKintosh

1995

FEBS Letters

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Whole cell extracts from rat liver or spinach leaves contain divalent ion-independent protein histidine phosphatase activity due to phosphatases of the PPIlPP2A family. In the rat liver extract, almost all the activity was found in the PP1, PP2A~ and PP2A2 peaks. In the spinach leaf extract, four phosphorylase phosphatase activity peaks were resolved --three containing PP1 and one containing PP2A --and all showed histidine phosphatase activity. Thus, protein histidine phosphatase activity is expressed in the cytosolic forms of protein phosphatases of the PPIlPP2A family in mammalian and plant cells.

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“…Other mammalian His kinases exist. Evidence for histone H4 His kinases (HHKs) activity has been found in regenerating rat liver, [20][21][22][23] foetal rat and human liver, 23 human hepatocarcinoma tissue, 23 pancreatic β cells, 24,25 thymus 26 and Walker-256 carcinosarcomas, 20,27 but have not been fully characterized or purified. Interestingly, HHKs from regenerating rat liver 21 and Walker-256-carcinosarcomas 27 each phosphorylated histone H4 leading to a τ-pHis residue.…”

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Advances in development of new tools for the study of phosphohistidine

Makwana

Muimo

Jackson

2018

Laboratory Investigation

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Protein phosphorylation is an important post-translational modification that is an integral part of cellular function. The O-phosphorylated amino-acid residues, such as phosphoserine (pSer), phosphothreonine (pThr) and phosphotyrosine (pTyr), have dominated the literature while the acid labile N-linked phosphorylated amino acids, such as phosphohistidine (pHis), have largely been historically overlooked because of the acidic conditions routinely used in amino-acid detection and analysis. This review highlights some misinterpretations that have arisen in the existing literature, pinpoints outstanding questions and potential future directions to clarify the role of pHis in mammalian signalling systems. Particular emphasis is placed on pHis isomerization and the hybrid functionality for both pHis and pTyr of the proposed τ-pHis analogue bearing the triazole residue.

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New Histone Kinases in Nuclei of Rat Tissues

Cited by 78 publications

References 13 publications

Protein histidine phosphorylation: Increased stability of thiophosphohistidine

Protein histidine phosphorylation: Increased stability of thiophosphohistidine

Protein histidine phosphatase activity in rat liver and spinach leaves

Advances in development of new tools for the study of phosphohistidine

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