Cloning and expression of diadenosine 5′,5‴-P1,P4-tetraphosphate hydrolase from Lupinus angustifolius L

Maksel, Danuta; Guranowski, Andrzej; Ilgoutz, C. Steven; Moir, Arthur J. G.; Blackburn, G. Michael; Gayler, R. Kenwyn

doi:10.1042/bj3290313

Cited by 42 publications

(40 citation statements)

References 40 publications

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“…DIPP represents the first hydrolase in the animal kingdom shown to prefer Ap 6 A and Ap 5 A over Ap 4 A. In fact, the kinetic parameters associated with DIPP-dependent Ap 6 A/Ap 5 A hydrolase activity are not only similar to those of Aps1 and YOR163w (Tables I and II), they are also in line with the characteristics of other MutT motif Ap n A hydrolases (25)(26)(27)(28)30). In that sense, DIPP is a typical Ap 6 A/Ap 5 A hydrolase.…”

Section: Discussionsupporting

confidence: 68%

The Diadenosine Hexaphosphate Hydrolases fromSchizosaccharomyces pombe and Saccharomyces cerevisiae Are Homologues of the Human Diphosphoinositol Polyphosphate Phosphohydrolase

Safrany¹,

Ingram²,

Cartwright³

et al. 1999

Journal of Biological Chemistry

131

133

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J. Biol. Chem. 274, 8604 -8610) have both previously been characterized as MutT family hydrolases with high specificity for diadenosine hexa-and pentaphosphates (Ap 6 A and Ap 5 A). Using purified recombinant preparations of these enzymes, we have now discovered that they have an important additional function, namely, the efficient hydrolysis of diphosphorylated inositol polyphosphates. This overlapping specificity of an enzyme for two completely different classes of substrate is not only of enzymological significance, but in addition, this finding provides important new information pertinent to the structure, function, and evolution of the MutT motif. Moreover, we report that the human protein previously characterized as a diphosphorylated inositol phosphate phosphohydrolase represents the first example, in any animal, of an enzyme that degrades Ap 6 A and Ap 5 A, in preference to other diadenosine polyphosphates. The emergence of Ap 6 A and Ap 5 A as extracellular effectors and intracellular ion-channel ligands points not only to diphosphorylated inositol phosphate phosphohydrolase as a candidate for regulating signaling by diadenosine polyphosphates, but also suggests that diphosphorylated inositol phosphates may competitively inhibit this process.Following the discovery of dinucleoside polyphosphates in biological systems over 30 years ago (1), these compounds have been studied extensively in prokaryotic and eukaryotic organisms. Several important intracellular and extracellular signaling functions have now been ascribed to the diadenosine compounds, Ap 3 A, 1 Ap 4 A, Ap 5 A, and Ap 6 A (2-4). Indeed, the ultimate fate of cell lineages and the very survival of an organism may depend upon the tight control of cellular diadenosine polyphosphate metabolism. For example, the intracellular level of Ap 4 A has long been known to be associated with cell proliferation (5). Moreover, it was recently proposed (6) that Ap 3 A has an antiproliferative role when complexed with the putative tumor suppressor Fhit protein, an Ap 3 A hydrolase (7,8). Thus, the Ap 3 A/Ap 4 A ratio may be an important factor in determining the alternative cellular fates of proliferation, differentiation, and apoptosis (3, 9). In higher eukaryotes, Ap n A appear also to be intracellular mediators of certain extracellular stimuli; they respond to glucose in pancreatic ␤-cells (10). Ap n A may also regulate ATP-sensitive K ϩ channels in ␤-cells and cardiac muscle (11-13) and intracellular ryanodine-binding Ca 2ϩ -release channels in cardiac and skeletal muscle, and in the brain (14, 15). Finally, extracellular Ap 5 A and Ap 6 A have also been identified as neurotransmitters (2) and vasomodulators (16,17).In addition to these physiological functions, Ap n A respond to heat shock and oxidative stress with an increase in concentration (18). If allowed to accumulate, they could prove toxic through their ability to inhibit nucleotide kinases (19,20), protein kinases (21,22), and other enzymes (23). Thus, there is considerable interest in the enzymes t...

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Section: Discussionsupporting

confidence: 68%

The Diadenosine Hexaphosphate Hydrolases fromSchizosaccharomyces pombe and Saccharomyces cerevisiae Are Homologues of the Human Diphosphoinositol Polyphosphate Phosphohydrolase

Safrany¹,

Ingram²,

Cartwright³

et al. 1999

Journal of Biological Chemistry

131

133

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“…The sequences corresponding to the mature chloroplastic AtNUDX26 showed 57.7% homology with that of AtNUDX27. Both AtNUDX26 and AtNUDX27 shared high similarity (69.8% and 59.2%, respectively) to a Nudix hydrolase that acts on asymmetric diadenosine tetraphosphates (Ap 4 A) from Lupinus angustifolius (Maksel et al, 1998). The deduced amino acid sequences of other predicted organelle-type AtNUDXs showed no significant homology to any conserved motifs, except the Nudix motif, in Nudix hydrolases from various organisms.…”

Section: Organelle-type Nudix Hydrolases In Arabidopsismentioning

confidence: 98%

Molecular Characterization of Organelle-Type Nudix Hydrolases in Arabidopsis

et al. 2008

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Nudix (for nucleoside diphosphates linked to some moiety X) hydrolases act to hydrolyze ribonucleoside and deoxyribonucleoside triphosphates, nucleotide sugars, coenzymes, or dinucleoside polyphosphates. Arabidopsis (Arabidopsis thaliana) contains 27 genes encoding Nudix hydrolase homologues (AtNUDX1 to -27) with a predicted distribution in the cytosol, mitochondria, and chloroplasts. Previously, cytosolic Nudix hydrolases (AtNUDX1 to -11 and -25) were characterized. Here, we conducted a characterization of organelle-type AtNUDX proteins (AtNUDX12 to -24, -26, and -27). AtNUDX14 showed pyrophosphohydrolase activity toward both ADP-ribose and ADP-glucose, although its K m value was approximately 100-fold lower for ADP-ribose (13.0 6 0.7 mM) than for ADP-glucose (1,235 6 65 mM). AtNUDX15 hydrolyzed not only reduced coenzyme A (118.7 6 3.4 mM) but also a wide range of its derivatives. AtNUDX19 showed pyrophosphohydrolase activity toward both NADH (335.3 6 5.4 mM) and NADPH (36.9 6 3.5 mM). AtNUDX23 had flavin adenine dinucleotide pyrophosphohydrolase activity (9.1 6 0.9 mM). Both AtNUDX26 and AtNUDX27 hydrolyzed diadenosine polyphosphates (n = 4-5). A confocal microscopic analysis using a green fluorescent protein fusion protein showed that AtNUDX15 is distributed in mitochondria and AtNUDX14 -19, -23, -26, and -27 are distributed in chloroplasts. These AtNUDX mRNAs were detected ubiquitously in various Arabidopsis tissues. The T-DNA insertion mutants of AtNUDX13,, and -27 did not exhibit any phenotypical differences under normal growth conditions. These results suggest that Nudix hydrolases in Arabidopsis control a variety of metabolites and are pertinent to a wide range of physiological processes.

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“…Enzymological and structural studies have shown that this arrangement of amino acids leads to a novel loop-helix-loop motif involved in substrate binding and catalysis (2)(3)(4)(5)(6)(7)(8). A recent BLAST (9) search of the data banks for the Nudix signature sequence has revealed over 800 open reading frames from more than 200 species including archaea, eubacteria, and eukarya, and at present, ϳ50 of the gene products have been identified.…”

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confidence: 99%

The Gene e.1 (nudE.1) of T4 Bacteriophage Designates a New Member of the Nudix Hydrolase Superfamily Active on Flavin Adenine Dinucleotide, Adenosine 5′-Triphospho-5′-adenosine, and ADP-ribose

Xu¹,

Gauss²,

Shen³

et al. 2002

Journal of Biological Chemistry

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The T4 bacteriophage gene e.1 was cloned into an expression vector and expressed in Escherichia coli, and the purified protein was identified as a Nudix hydrolase active on FAD, adenosine 5-triphospho-5-adenosine (Ap 3 A), and ADP-ribose. Typical of members of the Nudix hydrolases, the enzyme has an alkaline pH optimum (pH 8) and requires a divalent cation for activity that can be satisfied by Mg 2؉ or Mn 2؉ . For all substrates, AMP is one of the products, and unlike most of the other enzymes active on Ap 3 A, the T4 enzyme hydrolyzes higher homologues including Ap 4 -6 A. This is the first member of the Nudix hydrolase gene superfamily identified in bacterial viruses and the only one present in T4. The Nudix hydrolase superfamily consists of widely distributed subfamilies of enzymes characterized by a shared structural motif: the Nudix box having a highly conserved consensus sequence,where "X " represents any amino acid, and U usually represents one of the bulky, hydrophobic amino acids, Ile, Leu, or Val (1). Enzymological and structural studies have shown that this arrangement of amino acids leads to a novel loop-helix-loop motif involved in substrate binding and catalysis (2-8). A recent BLAST (9) search of the data banks for the Nudix signature sequence has revealed over 800 open reading frames from more than 200 species including archaea, eubacteria, and eukarya, and at present, ϳ50 of the gene products have been identified. These are all enzymes active on nucleoside diphosphate derivatives including (deoxy)nucleoside triphosphates, coenzymes, cell signaling molecules, and nucleotide sugars (1), and we have been systematically identifying and characterizing new members of the superfamily.An examination of the T4 bacteriophage genome reveals one gene, e

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Cloning and expression of diadenosine 5′,5‴-P1,P4-tetraphosphate hydrolase from Lupinus angustifolius L

Cited by 42 publications

References 40 publications

The Diadenosine Hexaphosphate Hydrolases fromSchizosaccharomyces pombe and Saccharomyces cerevisiae Are Homologues of the Human Diphosphoinositol Polyphosphate Phosphohydrolase

The Diadenosine Hexaphosphate Hydrolases fromSchizosaccharomyces pombe and Saccharomyces cerevisiae Are Homologues of the Human Diphosphoinositol Polyphosphate Phosphohydrolase

Molecular Characterization of Organelle-Type Nudix Hydrolases in Arabidopsis

The Gene e.1 (nudE.1) of T4 Bacteriophage Designates a New Member of the Nudix Hydrolase Superfamily Active on Flavin Adenine Dinucleotide, Adenosine 5′-Triphospho-5′-adenosine, and ADP-ribose

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