Effect of inorganic phosphate on synthesis of 5-phosphoribosyl-1-pyrophosphate in cultured plant cells

Ukaji, Toshiko; Ashihara, Hiroshi

doi:10.1016/0020-711x(87)90316-8

Cited by 20 publications

(7 citation statements)

References 25 publications

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“…In contrast, concentrations of free amino acids increased about sixfold (Table I). These results are consistent with those ofUkaji and Ashihara (14,15) tempt to convert the metabolite levels reported in Table I (Fig. 1).…”

Section: Resultssupporting

confidence: 83%

Phosphate Starvation Inducible `Bypasses' of Adenylate and Phosphate Dependent Glycolytic Enzymes in Brassica nigra Suspension Cells

Duff¹,

Moorhead²,

Lefebvre³

et al. 1989

Plant Physiol.

257

209

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When Brassica nigra leaf petiole suspension cells were subjected to 7 days of inorganic phosphate (Pi) starvation the extractable activity of: (a) pyrophosphate:fructose 6-phosphate 1-phosphotransferase, nonphosphorylating NADP-glyceraldehyde 3-phosphate dehydrogenase, phosphoenolpyruvate phosphatase, and phosphoenolpyruvate carboxylase increased at least fivefold, (b) phosphorylating NAD-glyceraldehyde 3-phosphate dehydrogenase decreased about sixfold, and (c) ATP:fructose 6-phosphate 1-phosphotransferase, 3-phosphoglycerate kinase, pyruvate kinase, or NAD malic enzyme was not altered. Pi deprivation also resulted in significant reductions in extractable levels of Pi, ATP, ADP, fructose 2,6-bisphosphate, and soluble protein, but caused a sixfold elevation in free amino acid concentrations. No change in inorganic pyrophosphate concentration was observed following Pi starvation. It is hypothesized that pyrophosphate:fructose 6-phosphate 1-phosphotransferase, nonphosphorylating NADP-glyceraldehyde 3-phosphate dehydrogenase, and phosphoenolpyruvate phosphatase bypass nucleotide phosphate or Pi-dependent glycolytic reactions during sustained periods of Pi depletion.

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Section: Resultssupporting

confidence: 83%

Phosphate Starvation Inducible `Bypasses' of Adenylate and Phosphate Dependent Glycolytic Enzymes in Brassica nigra Suspension Cells

Duff¹,

Moorhead²,

Lefebvre³

et al. 1989

Plant Physiol.

257

209

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“…In plants Le Floc'h (1984) also obtained substantia1 stimulation of PRS activity by Pi. However, Ashihara (1977), using spinach leaves, and Ukaji and Ashihara (1987), using PRS from C. roseus cells, found substantial inhibition of enzymatic activity by Pi. The results obtained on H. brasiliensis latex PRS would seem to explain these apparently contradictory results.…”

Section: Discussionmentioning

confidence: 99%

Purification and Characterization of Phosphoribosylpyrophosphate Synthetase from Rubber Tree Latex

et al. 1997

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“…The findings of Figure 1 indicate that the true substrate for the maize root H ϩ -PPase was the very low PP i concentration derived from Reaction 1 and that the P i released into the medium originated from F1,6BP by the action of PFP, which continuously regenerated the PP i hydrolyzed (Reactions 1 and 2). (Rebeille et al, 1983;Ukaji and Ashihara, 1987;Weiner et al, 1987;Kubota and Ashihara, 1990;Davies et al, 1993;Stitt, 1998).…”

Section: Cleavage Of F16bp Ph and Mgmentioning

confidence: 99%

“…b The molar concentrations of F1,6BP, P i , and F6P are those reported in the literature for plant cell cytosol (Rebeille et al, 1983;Ukaji and Ashihara, 1987;Weiner et al, 1987;Kubota and Ashihara, 1990;Davies et al, 1993;Stitt, 1998).…”

Section: Table II Pp I Formation In Presence Of F16bp P I and F6pmentioning

confidence: 99%

“…The aim of this study was to evaluate whether the maize (Zea mays) root H ϩ -PPase is able to bind and hydrolyze the PP i formed by Reaction 1 catalyzed by PFP in vitro under conditions that mimic the concentrations of F1,6BP, P i , Mg 2ϩ , F2,6BP, and F6P found in the plant cell cytosol (Rebeille et al, 1983;Ukaji and Ashihara, 1987;Weiner et al, 1987;Kubota and Ashihara, 1990;Davies et al, 1993;Stitt, 1998; Table I). Here, we show that the affinity of maize root H ϩ -PPase for PP i under these conditions is sufficient to shift Reaction 1 toward PP i formation, making it possible to build up a proton gradient in the tonoplast even in the presence of very low amounts of PFP.…”

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confidence: 99%

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Proton Transport in Maize Tonoplasts Supported by Fructose-1,6-Bisphosphate Cleavage. Pyrophosphate-Dependent Phosphofructokinase as a Pyrophosphate-Regenerating System

et al. 2003

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The energy derived from pyrophosphate (PP i ) hydrolysis is used to pump protons across the tonoplast membrane, thus forming a proton gradient. In a plant's cytosol, the concentration of PP i varies between 10 and 800 m, and the PP i concentration needed for one-half maximal activity of the maize (Zea mays) root tonoplast H ϩ -pyrophosphatase is 30 m. In this report, we show that the H ϩ -pyrophosphatase of maize root vacuoles is able to hydrolyze PP i (Reaction 2) formed by Reaction 1, which is catalyzed by PP i -dependent phosphofructokinase (PFP):Fructose-1,6-bisphosphate (F1,6BP) ϩ P i 7 PP i ϩFructose-6-phosphate (F6 P) (reaction 1)During the steady state, one-half of the inorganic phosphate released (Reaction 4) is ultimately derived from F1,6BP, whereas PFP continuously regenerates the pyrophosphate (PP i ) hydrolyzed. A proton gradient (⌬pH) can be built up in tonoplast vesicles using PFP as a PP i -regenerating system. The ⌬ pH formed by the H ϩ -pyrophosphatase can be dissipated by addition of 20 mm F6P, which drives Reaction 1 to the left and decreases the PP i available for the H ϩ -pyrophosphatase. The maximal ⌬ pH attained by the pyrophosphatase coupled to the PFP reaction can be maintained by PFP activities far below those found in higher plants tissues.

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Effect of inorganic phosphate on synthesis of 5-phosphoribosyl-1-pyrophosphate in cultured plant cells

Cited by 20 publications

References 25 publications

Phosphate Starvation Inducible `Bypasses' of Adenylate and Phosphate Dependent Glycolytic Enzymes in Brassica nigra Suspension Cells

Phosphate Starvation Inducible `Bypasses' of Adenylate and Phosphate Dependent Glycolytic Enzymes in Brassica nigra Suspension Cells

Purification and Characterization of Phosphoribosylpyrophosphate Synthetase from Rubber Tree Latex

Proton Transport in Maize Tonoplasts Supported by Fructose-1,6-Bisphosphate Cleavage. Pyrophosphate-Dependent Phosphofructokinase as a Pyrophosphate-Regenerating System

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