Influence of light on phosphoenol pyravate carboxylase in sorghum leaves

Vidal, Jean; Godbillon, G.; Gadal, Pierre

doi:10.1111/j.1399-3054.1983.tb00741.x

Cited by 22 publications

(9 citation statements)

References 13 publications

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“…activity was paralleled by the accumulation of large amounts of PEPC in the leaf (3,9,11,17,28). These results were further extended by Sims and Hague (8,21) who observed a photoinduced increase in translatable mRNA upon greening of maize leaf, and then by Harpster and Taylor (10) who quantitatively characterized the specific mRNA in maize leaf extracts.…”

supporting

confidence: 61%

“…The E-PEPC is present in etiolated leaves and displays functional and regulatory properties similar to C3-type PEPC. The G-PEPC is a C4 photosynthetic type ofPEPC which is present in green leaves and possesses specific functional, chromatographic, physicochemical, and immunochemical properties (25,28,29). The use of monoclonal antibodies specific for the G-PEPC showed that it was the lightactivated isozyme and that no conversion mechanism was responsible for the observed polymorphism (23).…”

mentioning

confidence: 99%

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Photocontrol of Sorghum Leaf Phosphoenolpyruvate Carboxylase

Thomas

Crétin²,

Kéryer³

et al. 1987

Plant Physiol.

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supporting

confidence: 61%

mentioning

confidence: 99%

Photocontrol of Sorghum Leaf Phosphoenolpyruvate Carboxylase

Thomas

Crétin²,

Kéryer³

et al. 1987

Plant Physiol.

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“…For AGPase detection, an antibody raised against recombinant potato AGPase (Tiessen et al, 2002) was used. The PEPCase antibody was raised against the purified sorghum (Sorghum vulgare) enzyme (Vidal et al, 1983). The GWD antibody was raised against the purified protein from potato (Ritte et al, 2000a).…”

Section: Antibodiesmentioning

confidence: 99%

Identification of a Novel Enzyme Required for Starch Metabolism in Arabidopsis Leaves. The Phosphoglucan, Water Dikinase

Pusch²,

et al. 2005

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The phosphorylation of amylopectin by the glucan, water dikinase (GWD; EC 2.7.9.4) is an essential step within starch metabolism. This is indicated by the starch excess phenotype of GWD-deficient plants, such as the sex1-3 mutant of Arabidopsis (Arabidopsis thaliana). To identify starch-related enzymes that rely on glucan-bound phosphate, we studied the binding of proteins extracted from Arabidopsis wild-type leaves to either phosphorylated or nonphosphorylated starch granules. Granules prepared from the sex1-3 mutant were prephosphorylated in vitro using recombinant potato (Solanum tuberosum) GWD. As a control, the unmodified, phosphate free granules were used. An as-yet uncharacterized protein was identified that preferentially binds to the phosphorylated starch. The C-terminal part of this protein exhibits similarity to that of GWD. The novel protein phosphorylates starch granules, but only following prephosphorylation with GWD. The enzyme transfers the b-P of ATP to the phosphoglucan, whereas the g-P is released as orthophosphate. Therefore, the novel protein is designated as phosphoglucan, water dikinase (PWD). Unlike GWD that phosphorylates preferentially the C6 position of the glucose units, PWD phosphorylates predominantly (or exclusively) the C3 position. Western-blot analysis of protoplast and chloroplast fractions from Arabidopsis leaves reveals a plastidic location of PWD. Binding of PWD to starch granules strongly increases during net starch breakdown. Transgenic Arabidopsis plants in which the expression of PWD was reduced by either RNAi or a T-DNA insertion exhibit a starch excess phenotype. Thus, in Arabidopsis leaves starch turnover requires a close collaboration of PWD and GWD.

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“…Vidal and Gadal (18) and Vidal et al (19) found that two isoforms of PEPC' were present in etiolated leaves of sorghum. One form, found in the eitolated leaves, was designated E-PEPC.…”

Section: Introductionmentioning

confidence: 99%

“…Sucrose synthesis is apparently the only physiological function ofsucrose-P synthase, with the equilibrium constant for sucrose synthesis about 2 (1). This makes sucrose-P synthase a focal point for studying regulation of sucrose metabolism and partitioning.Vidal and Gadal (18) and Vidal et al (19) found that two isoforms of PEPC' were present in etiolated leaves of sorghum. One form, found in the eitolated leaves, was designated E-PEPC.…”

mentioning

confidence: 99%

Phytochrome Mediated Regulation of Sucrose Phosphate Synthase Activity in Maize

Vassey

1988

Plant Physiol.

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The extractable activity of sucrose phosphate synthase was determined in etiolated seedlings of maize (Zea mays L.), soybean (Glycine max [L.] Merr.), and sugar beet (Beta vulgaris L.) following treatments of changing light quality. A 30-minute illumination of 30 microeinsteins per square meter per second white light produced a three-fold increase in sucrose phosphate synthase activity at 2 hours postillumination when compared to seedlings maintained in total darkness. Etiolated maize seedlings treated with 3.6 microeinsteins per square meter per second of red and far-red light showed a 50% increase and a 50% decrease in sucrose phosphate synthase activity, respectively, when compared to etiolated maize seedlings treated with white light. Maize seedlings exposed for 30 minutes to red followed by 30 minutes to far-red showed an initial increase in sucrose phosphate synthase activity followed by a rapid decrease to control level. Neither soybean or sugar beet sucrose phosphate synthase responded to the 30-minute illumination of white light. Phytochrome is involved in sucrose phosphate synthase regulation in maize, whereas it is not responsible for changes in sucrose phosphate synthase activity in soybean or sugar beet.Sucrose-P synthase appears to be a major control point in sucrose formation during photoassimilation of CO2 (10). Sucrose synthesis is apparently the only physiological function ofsucrose-P synthase, with the equilibrium constant for sucrose synthesis about 2 (1). This makes sucrose-P synthase a focal point for studying regulation of sucrose metabolism and partitioning.Vidal and Gadal (18) and Vidal et al. (19) found that two isoforms of PEPC' were present in etiolated leaves of sorghum. One form, found in the eitolated leaves, was designated E-PEPC. The other form found in greening leaves was designated G-PERPC and occurred only after etiolated leaves were exposed to light. Later, Thomas et al. (16) showed that the activity of G-PEPC was sensitive to red and far-red treatments. A 10-min exposure to red stimulated G-PEPC, whereas far-red (either alone or following a red treatment) caused a substantial inhibition of the G-PEPC isoform. They concluded from these experiments that phytochrome was the photoreceptor triggering changes in enzyme activity.The present study was designed to examine the role of light ' Abbreviations: PEPC, phosphoenolpyruvate carboxylase; G6P, glucose 6-phosphate; UDPG, uridine 5'-diphosphoglucose; PPFD, photosynthetic photon flux density. quality on the extractable activity of sucrose-P synthase in maize, soybean, and sugar beets. This was done using 10-day-old seedlings of each species grown in total darkness and illuminating them with white light, red, far-red, or red followed by far red. MATERIALS AND METHODSPlant Materials. Maize (Zea mays L., cv FS854), soybean (Glycine max. [L.] Merr., cv Pioneer 1082), and sugar beet (Beta vulgaris L., cv Great Western multigerm hybrid) seeds were germinated in darkness then planted in 7 cm x 7 cm plastic pots containing ver...

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Influence of light on phosphoenol pyravate carboxylase in sorghum leaves

Cited by 22 publications

References 13 publications

Photocontrol of Sorghum Leaf Phosphoenolpyruvate Carboxylase

Photocontrol of Sorghum Leaf Phosphoenolpyruvate Carboxylase

Identification of a Novel Enzyme Required for Starch Metabolism in Arabidopsis Leaves. The Phosphoglucan, Water Dikinase

Phytochrome Mediated Regulation of Sucrose Phosphate Synthase Activity in Maize

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