Protein histidine phosphatase activity in rat liver and spinach leaves

Matthews, Harry R.; MacKintosh, Carol

doi:10.1016/0014-5793(95)00353-b

Cited by 20 publications

(13 citation statements)

References 49 publications

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“…The fortunate choice of the phosphohistidine-containing peptide Suc-Ala-His(P)-Pro-Phe-pNA (phosphopeptide I) as the probing substrate was essential for this outcome. Phosphatases 1, 2A and 2C represent most of the protein phosphohistidine phosphatase activity in liver cytosol when assayed with 5 lM phosphohistidine-containing histone H4 [29]. This activity was about twofold higher than that observed in the present work using phosphopeptide I.…”

Section: Discussioncontrasting

confidence: 77%

Identification and characterization of a mammalian 14‐kDa phosphohistidine phosphatase

Pettersson

et al. 2002

European Journal of Biochemistry

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Protein histidine phosphorylation in eukaryotes has been sparsely studied compared to protein serine/threonine and tyrosine phosphorylation. In an attempt to rectify this by probing porcine liver cytosol with the phosphohistidinecontaining peptide succinyl-Ala-His(P)-Pro-Phe-p-nitroanilide (phosphopeptide I), we observed a phosphatase activity that was insensitive towards okadaic acid and EDTA. This suggested the existence of a phosphohistidine phosphatase different from protein phosphatase 1, 2A and 2C. A 1000-fold purification to apparent homogeneity gave a 14-kDa phosphatase with a specific activity of 3 lmolAEmin )1 AEmg )1 at pH 7.5 with 7 lM phosphopeptide I as substrate. Partial amino-acid sequence determination of the purified porcine enzyme by MS revealed similarity with a human sequence representing a human chromosome 9 gene of hitherto unknown function. Molecular cloning from a human embryonic kidney cell cDNAlibrary followed by expression and purification, yielded a protein with a molecular mass of 13 700 Da, and an EDTA-insensitive phosphohistidine phosphatase activity of 9 lmolAEmin )1 AEmg )1 towards phosphopeptide I. No detectable activity was obtained towards a set of phosphoserine-, phosphothreonine-, and phosphotyrosine peptides. Northern blot analysis indicated that the human phosphohistidine phosphatase mRNA was present preferentially in heart and skeletal muscle. These results provide a new tool for studying eukaryotic histidine phosphorylation/dephosphorylation.Keywords: dephosphorylation; N-phosphorylation; phosphoamidase; phosphopeptide; protein histidine phosphatase.Boyer and coworkers detected protein-bound phosphohistidine in rat-liver mitochondrial succinyl-CoA synthetase almost 40 years ago [1,2]. Despite the long time interval and the fact that phosphohistidine represents a substantial fraction of eukaryotic protein-bound phosphate [3], only a few phosphohistidine-containing proteins have been detected compared to the large number of eukaryotic proteins phosphorylated on serine, threonine and tyrosine residues. One reason for this difference may be that the N-bound phosphate of phosphohistidine easily escapes detection by common analytical procedures, due to its lability under acidic conditions, e.g. during fixation and staining of gels after SDS/PAGE [4].The studies on eukaryotic protein histidine phosphorylation and dephosphorylation have dealt with essentially two aspects. One is the intermediary phosphorylation of enzymes [5][6][7][8][9][10], of which nucleoside diphosphate kinase is a particularly well-studied example. The other is the reversible protein histidine phosphorylation by protein kinases and phosphatases [3,11]. An important contribution to the latter field was the purification of a yeast protein histidine kinase in 1991 [12]. Access to this enzyme also made possible the preparation of 32 P-labelled histone H4, which was later used as substrate in the search for phosphohistidine phosphatases. Using such an approach, the catalytic subunits of the well-studied serine/...

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Section: Discussioncontrasting

confidence: 77%

Identification and characterization of a mammalian 14‐kDa phosphohistidine phosphatase

Pettersson

et al. 2002

European Journal of Biochemistry

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“…The PPP catalytic domain spans ~270 amino acids and some of the invariant residues play crucial roles in binding divalent metal ions, while others interact with the substrate's phosphate group. Although PPPs mainly act upon phosphoserine and phosphothreonine residues, other phospho amino acids such as phosphohistidine can be dephosphorylated by some PPP family members such as Ppp1 and Ppp2/PP2A (Matthews and MacKintosh 1995). The carboxy-terminal region of the catalytic domain contains a conserved motif -SAxNY-that lies in a flexible loop region and in some Ppps has been implicated in the binding of a number of naturally occurring tumour promoters and toxins, such as okadaic acid found in shellfish and microcystin produced by blue green algae (Table 2) (Holmes et al…”

Section: Phylogenetic and Structural Relationships In The Ppp Familymentioning

confidence: 99%

Overview of protein serine/threonine phosphatases

Cohen

2003

Protein Phosphatases

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Protein phosphatases that cleave phosphate from phosphorylated serine and threonine in proteins are crucial for the regulation of most cellular processes. Three structurally distinct families of protein serine/threonine phosphatases (PPP, PPM, and FCP) are described and the phylogenetic relationships in the PPP and PPM families of Homo sapiens, Drosophila melanogaster, and Saccharomyces cerevisiae are examined. An overview of the functions of the PPP, PPM, and FCP members gained from recent genetic analyses is presented. Protein serine/threonine phosphatases and their classificationThe past two decades of cDNA and genome sequencing has uncovered nearly 30 bona fide human protein serine/threonine phosphatase catalytic subunit genes. These encode enzymes that catalyse the cleavage of phosphate from serine and threonine residues in proteins that have been phosphorylated by protein kinases. Despite the fact that virtually all the more than 300 serine/threonine kinases are members of the same family, the serine/threonine phosphatases comprise three distinct families, which are structurally distinct from the family of protein tyrosine phosphatases that encompasses the tyrosine and dual specificity (tyrosine and serine/threonine) phosphatases. The current classification of protein serine/threonine protein phosphatases is based upon the amino acid sequences of their catalytic subunits. The PPP family includes the prototypic member protein phosphatase 1 (PP1/Ppp1c), while the PPM family is represented by protein phosphatase 2C (PP2C/Ppm1) and the FCP family was more recently recognised through its founding member (Fcp1), which dephosphorylates the carboxy-terminal domain of RNA polymerase II (Table 1). Members of the three families are widely distributed among eukaryotic phyla ( Fig. 1 and 2) and prokaryotes usually contain at least one PPP and/or PPM phosphatase (Kennelly 2002;Cohen 2003).

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“…42 In addition, pHis phosphatase activity has been reported in rat tissue extracts but these have not been fully characterized. [43][44][45][46] Not only is His phosphorylation predicted to be prevalent in eukaryotic proteins, 38 it has also been associated with important mammalian cellular processes. For example, pHis has been shown to be present in heteromeric G proteins (GNB1), which are involved in G protein signalling, 15,47,48 KCa3.1 potassium channel, which is involved in ion conductance, 18,49 ATP-citrate lyase (ACLY), which is involved in cell metabolism, 9 histone H4, which is involved in chromatin biology, 21,22,28 transient receptor potentialvanilloid-5 (TRPV5), which regulates urinary Ca 2+ excretion, 17 and phosphoglycerate mutase 1 (PGAM1), which is involved in glycolysis.…”

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confidence: 99%

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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Protein histidine phosphatase activity in rat liver and spinach leaves

Cited by 20 publications

References 49 publications

Identification and characterization of a mammalian 14‐kDa phosphohistidine phosphatase

Identification and characterization of a mammalian 14‐kDa phosphohistidine phosphatase

Overview of protein serine/threonine phosphatases

Advances in development of new tools for the study of phosphohistidine

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