Characterization of diphosphonucleotide phosphatase/phosphodiesterase from yellow lupin (Lupinus luteus) seeds

Olczak, Mariusz; Kobiałka, Marcin; Watorek, W

doi:10.1016/s0167-4838(00)00024-8

Cited by 27 publications

(32 citation statements)

References 23 publications

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“…Various phosphodiesterases have already been reported in the vacuole (Nishimura and Beevers, 1978;Boller and Kende, 1979) and in the extracellular compartments (Abel et al, 2000;Olczak et al, 2000;Rodriguez-Lopez et al, 2001). However, none of these authors reported a specific action on glycerophosphodiesters.…”

Section: Originality Of Plant Gpc-pdementioning

confidence: 98%

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Glycerophosphocholine Metabolism in Higher Plant Cells. Evidence of a New Glyceryl-Phosphodiester Phosphodiesterase

et al. 2002

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Glycerophosphocholine (GroPCho) is a diester that accumulates in different physiological processes leading to phospholipid remodeling. However, very little is known about its metabolism in higher plant cells. 31 P-Nuclear magnetic resonance spectroscopy and biochemical analyses performed on carrot (Daucus carota) cells fed with GroPCho revealed the existence of an extracellular GroPCho phosphodiesterase. This enzymatic activity splits GroPCho into sn-glycerol-3-phosphate and free choline. In vivo, sn-glycerol-3-phosphate is further hydrolyzed into glycerol and inorganic phosphate by acid phosphatase. We visualized the incorporation and the compartmentation of choline and observed that the major choline pool was phosphorylated and accumulated in the cytosol, whereas a minor fraction was incorporated in the vacuole as free choline. Isolation of plasma membranes, culture medium, and cell wall proteins enabled us to localize this phosphodiesterase activity on the cell wall. We also report the existence of an intracellular glycerophosphodiesterase. This second activity is localized in the vacuole and hydrolyzes GroPCho in a similar fashion to the cell wall phosphodiesterase. Both extra-and intracellular phosphodiesterases are widespread among different plant species and are often enhanced during phosphate deprivation. Finally, competition experiments on the extracellular phosphodiesterase suggested a specificity for glycerophosphodiesters (apparent K m of 50 m), which distinguishes it from other phosphodiesterases previously described in the literature.Phospholipids play a key role in the architecture of eukaryote membranes. Membrane lipid composition is under tight regulation that involves both lipid biosynthesis and turnover. Phospholipid turnover may result from the action of acyl-transferases (Frentzen, 1993), phospholipases (Wang, 1993;Munnik et al., 1998), or lipolytic acyl-hydrolases (Huang, 1993. Among the catabolic products, acyl groups can be degraded by ␣-or ␤-oxidation and used as a respiratory substrates (Gerhardt, 1993) or for triacylglycerol synthesis (Frentzen, 1993;Ohlrogge and Browse, 1995). The phospholipid head groups are a source of glycerol, phosphate, or polar head moieties that can be reused directly in phospholipid synthesis (Kinney, 1993).In non-plant eukaryotes, phospholipid catabolism often produces glycerophosphodiesters. In yeast (Saccharomyces cerevisiae), glycerophosphodiesters are secreted in the extracellular medium and hydrolyzed at the outer surface of the cell (Patton et al., 1995;Dowd et al., 2001). In animal cells, glycerophosphodiesters, mainly glycerophosphocholine (GroPCho) are synthesized from phospholipids. In HeLa cells, GroPCho secretion was observed (Barburina and Jackowski, 1999). Moreover, GroPCho can accumulate in renal cells where its role as an osmoprotectant has been suggested (Zablocki et al., 1991; Bauernschmitt and Kinne, 1993). GroPCho concentration in renal cells is controlled by its enzymatic degradation rate, involving phosphodiesterase (Zablocki et al., 1...

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Section: Originality Of Plant Gpc-pdementioning

confidence: 98%

“…Phosphodiesterases have been described recently in the cell wall or in the extracellular medium (Abel et al, 2000;Olczak et al, 2000;Rodriguez-Lopez et al, 2000. Most were reported to split the artificial substrate bis-p-nitrophenyl phosphate (bis-PNPP).…”

Section: Substrate Specificity Of Gpc-pde Activitymentioning

confidence: 99%

Glycerophosphocholine Metabolism in Higher Plant Cells. Evidence of a New Glyceryl-Phosphodiester Phosphodiesterase

et al. 2002

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“…Moreover, NPP1 shares sequence Numbers 1 to 6 correspond to Figure 1 (left panel). similarity with PPD1, a metallophosphatase from yellow lupin that specifically cleaves the pyrophosphate bond of diphosphonucleotides such as ADP and GDP (Olczak et al, 2000;Olczak and Olczak, 2002). Unlike barley and rice NPPs, however, PPD1 is presented as a monomer, has strong affinity toward nucleoside diphosphates, and does not split the pyrophosphate linkage of nucleotide sugars.…”

Section: Rice and Barley Adpg Hydrolytic Npps Are Members Of A Ubiquimentioning

confidence: 99%

Rice PlastidialN-Glycosylated Nucleotide Pyrophosphatase/Phosphodiesterase Is Transported from the ER-Golgi to the Chloroplast through the Secretory Pathway

et al. 2006

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A nucleotide pyrophosphatase/phosphodiesterase (NPP) activity that catalyzes the hydrolytic breakdown of ADP-glucose (ADPG) has been shown to occur in the plastidial compartment of both mono-and dicotyledonous plants. To learn more about this enzyme, we purified two NPPs from rice (Oryza sativa) and barley (Hordeum vulgare) seedlings. Both enzymes are glycosylated, since they bind to concanavalin A, stain with periodic acid-Schiff reagent, and are digested by Endo-H. A complete rice NPP cDNA, designated as NPP1, was isolated, characterized, and overexpressed in transgenic plants displaying high ADPG hydrolytic activity. Databank searches revealed that NPP1 belongs to a functionally divergent group of plant nucleotide hydrolases. NPP1 contains numerous N-glycosylation sites and a cleavable hydrophobic signal sequence that does not match with the N-terminal part of the mature protein. Both immunocytochemical analyses and confocal fluorescence microscopy of rice cells expressing NPP1 fused with green fluorescent protein (GFP) revealed that NPP1-GFP occurs in the plastidial compartment. Brefeldin A treatment of NPP1-GFP-expressing cells prevented NPP1-GFP accumulation in the chloroplasts. Endo-H digestibility studies revealed that both NPP1 and NPP1-GFP in the chloroplast are glycosylated. Collectively, these data demonstrate the trafficking of glycosylated proteins from the endoplasmic reticulum-Golgi system to the chloroplast in higher plants.

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“…Acid Phosphatases (ACP) are a group of enzymes that catalyze the hydrolysis of a variety of phosphate esters. These enzymes are widely distributed in plants and are related to phosphate supply and metabolism from a vast array of phosphate esters which are essential for normal growth and development of plant organs (Olczak et al, 2000). The present work revealed that amount of increment in saline grown plant occurred ranging from 139 -293%.…”

Section: Discussionmentioning

confidence: 59%

Salinity Dependent Photosynthetic Response and Regulation of Some Enzymes in Halophytes from Indian Sundarbans

Das¹

2012

Applied Photosynthesis

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Characterization of diphosphonucleotide phosphatase/phosphodiesterase from yellow lupin (Lupinus luteus) seeds

Cited by 27 publications

References 23 publications

Glycerophosphocholine Metabolism in Higher Plant Cells. Evidence of a New Glyceryl-Phosphodiester Phosphodiesterase

Glycerophosphocholine Metabolism in Higher Plant Cells. Evidence of a New Glyceryl-Phosphodiester Phosphodiesterase

Rice PlastidialN-Glycosylated Nucleotide Pyrophosphatase/Phosphodiesterase Is Transported from the ER-Golgi to the Chloroplast through the Secretory Pathway

Salinity Dependent Photosynthetic Response and Regulation of Some Enzymes in Halophytes from Indian Sundarbans

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