Effect of Light and NO3− on Wheat Leaf Phosphoenolpyruvate Carboxylase Activity

Quy, Le Van; Foyer, Christine H.; Champigny, Marie‐Louise

doi:10.1104/pp.97.4.1476

Cited by 107 publications

(89 citation statements)

References 20 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…wheat seedlings (Van Quy et al, 1991;Manh et al, 1993;. The present study with tobacco has established that the regulatory phosphorylation of this ubiquitous plant enzyme also occurs in leaves of an Nsufficient C, plant.…”

Section: Gin Is Involved In the Light Activation Of Tobacco-leaf Pepcmentioning

confidence: 89%

“…However, information concerning how the phosphorylation of the C, isoforms is regulated in response to environmental signals is limited. For example, although previous studies (Van Quy et al, 1991; showed that PEPC in N-deficient wheat leaves is subject to regulatory phosphorylation, it is unclear whether the enzyme in leaves of N-sufficient C, plants is also influenced by this same mode of regulation (Rajagopalan et al, 1993;Gupta et al, 1994;. Similarly, although there has been speculation that the phosphorylation state of PEPC in C, leaves is controlled largely by PEPC-PK (Champigny, 1995), as it is in C, and CAM plants, its experimental basis is weak.…”

mentioning

confidence: 96%

“…Van Quy et al (1991) and, more recently, found that illumination and nitrate feeding of excised, N-deficient wheat leaves increased the activity and I B 0 (~-malate) of PEPC, which was accompanied by an increased in vivo incorporation of 32P from radioactive Pi into the enzyme. The regulation of PEPC by reversible phosphorylation in Vicia guard cells and soybean Plant Physiol.…”

mentioning

confidence: 99%

“…Similarly, although there has been speculation that the phosphorylation state of PEPC in C, leaves is controlled largely by PEPC-PK (Champigny, 1995), as it is in C, and CAM plants, its experimental basis is weak. Except in one recent investigation in which PEPC-kinase activity was surveyed in N-deficient wheat leaves , neither protein-kinase nor protein-phosphatase activity has been studied directly in C, plants; instead, changes in the activity and/or L-malate sensitivity of PEPC have been used as an indicator for apparent changes in PEPC-PK activity (Van Quy et al, 1991;Manh et al, 1993). Obviously, direct and more detailed studies of C, PEPC-kinase are needed to document that this protein-Ser /Thr kinase, indeed, controls the phosphorylation state of PEPC in C, plants and to begin to understand the signal-transduction pathway leading to the reversible phosphorylation of this target protein in N-sufficient C, leaves.…”

mentioning

confidence: 99%

See 3 more Smart Citations

Phosphoenolpyruvate Carboxylase Kinase in Tobacco Leaves Is Activated by Light in a Similar but Not Identical Way as in Maize

Zhang

Chollet

1996

Plant Physiology

View full text Add to dashboard Cite

We have previously reported the partial purification of a Ca2+- independent phosphoenolpyruvate carboxylase (PEPC) protein-serine/threonine kinase (PEPC-PK) from illuminated leaves of N-sufficient tobacco (Nicotiana tabacum L.) plants (Y.-H. Wang, R. Chollet [1993] FEBS Lett 328: 215–218). We now report that this C3 PEPC-kinase is reversibly light activated in vivo in a time-dependent manner. As the kinase becomes light activated, the activity and L-malate sensitivity of its target protein increases and decreases, respectively. The light activation of tobacco PEPC-PK is prevented by pretreatment of detached leaves with various photosynthesis and cytosolic protein-synthesis inhibitors. Similarly, specific inhibitors of glutamine synthetase block the light activation of tobacco leaf PEPC-kinase under both photorespiratory and nonphotorespiratory conditions. This striking effect is partially and specifically reversed by exogenous glutamine, whereas it has no apparent effect on the light activation of the maize (Zea mays L.) leaf kinase. Using an in situ “activity-gel” phosphorylation assay, we have identified two major Ca2+-independent PEPC-kinase catalytic polypeptides in illuminated tobacco leaves that have the same molecular masses (approximately 30 and 37 kD) as found in illuminated maize leaves. Collectively, these results indicate that the phosphorylation of PEPC in N-sufficient leaves of tobacco (C3) and maize (C4) is regulated through similar but not identical light-signal transduction pathways.

show abstract

Section: Gin Is Involved In the Light Activation Of Tobacco-leaf Pepcmentioning

confidence: 89%

mentioning

confidence: 96%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

Phosphoenolpyruvate Carboxylase Kinase in Tobacco Leaves Is Activated by Light in a Similar but Not Identical Way as in Maize

Zhang

Chollet

1996

Plant Physiology

View full text Add to dashboard Cite

show abstract

“…It has been shown that they are subject to allosteric control (Andreo et al, 1987), but there is little experimental evidence to illustrate the in vivo posttranslational regulation, the signal transduction pathway, and the nature of the stimulus operating on the covalent modification of these nonphotosynthetic isoforms. The nonphotosynthetic PEPCs were shown to be in vivo phosphorylated in illuminated, N-recovering wheat (Trificum aestivum) leaves (Van Quy et al, 1991;Van Quy and Champigny, 1992;, in soybean nodules (Zhang et al, 1995), and in stomatal guard cells (Schnabl et al, 1992;Zhang et al, 1994). Changes in the properties of an in vitro phosphorylated enzyme were established only for the recombinant C,-type Sorghum PEPC (Pacquit et al, 1993) and the soybean nodule enzyme (Schuller and Dietrich, 1993).…”

mentioning

confidence: 99%

In Vivo and in Vitro Phosphorylation of the Phosphoenolpyruvate Carboxylase from Wheat Seeds during Germination

et al. 1996

View full text Add to dashboard Cite

Phosphoenolpyruvate carboxylase (PEPC) activity was detected in the aleurone endosperm of wheat (Triticum aestivum cv Chinese Spring) seeds, and specific anti-Sorghum C, PEPC polyclonal antibodies cross-reacted with 103-and 100-kD polypeptides present in dry seeds and seeds that had imbibed; in addition, a new, 108-kD polypeptide was detected 6 h after imbibition. l h e use of specific anti-phosphorylation-site immunoglobulin C (APS-lgC) identified the presence of a phosphorylation motif equivalent to that found in other plant PEPCs studied so far. The binding of this APS-lgC to the target protein promoted changes in the properties of seed PEPC similar to those produced by phosphorylation, as previously shown for the recombinant Sorghum leaf C, PEPC. In desalted seed extracts, an endogenous PEPC kinase activity catalyzed a bona fide phosphorylation of the target protein, as deduced from the immunoinhibition of the in vitro phosphorylation reaction by the APSIgC. In addition, the major, 103-kD PEPC polypeptide was also shown to be radiolabeled in situ 48 h after imbibition in [32Plorthophosphate. The ratio between optimal (pH 8) and suboptimal (pH 7.3 or 7.1) PEPC activity decreased during germination, thereby suggesting a change in catalytic rate related to an in vivo phosphorylation process. These collective data document that the components needed for the regulatory phosphorylation of PEPC are present and functional during germination of wheat seeds.

show abstract

Mitochondrial Redox State, Nitrogen Metabolism and Signalling

Foyer

2018

Annual Plant Reviews Online

View full text Add to dashboard Cite

Nitrogen is often a limiting factor for plant growth and development, and therefore there is considerable interest and potential agronomic benefit not only in understanding the mechanisms that determine nitrogen use efficiency (NUE) but also in identifying new targets for NUE improvement. Much attention in recent years has focused on the core pathways and enzymes involved in primary nitrogen assimilation as well as the processes of N uptake and transport. However, recent studies on mitochondrial Complex I mutants indicate that enzymes involved in energy metabolism in the mitochondria could also be useful targets for improving NUE. TheNicotiana sylvestriscytoplasmic male sterile II (CMSII) mutant lacks respiratory Complex I, but high rates of respiration are sustained because of the presence of alternative NADH dehydrogenases. The CMSII mutation has striking effects on leaf amino acids, which are the focal point around which primary N assimilation and associated carbon metabolism and photorespiration and export occur, and on pyridine nucleotides, which are essential for metabolism and signalling. The absence of major mitochondrial NADH dehydrogenase (Complex I) in the CMSII mutant results in an N‐rich phenotype and altered N signalling. Adjustments in the abundance of Complex I relative to the alternative NADH dehydrogenases could therefore provide a mechanism for improved NUE.

show abstract

Effect of Light and NO₃⁻ on Wheat Leaf Phosphoenolpyruvate Carboxylase Activity

Cited by 107 publications

References 20 publications

Phosphoenolpyruvate Carboxylase Kinase in Tobacco Leaves Is Activated by Light in a Similar but Not Identical Way as in Maize

Phosphoenolpyruvate Carboxylase Kinase in Tobacco Leaves Is Activated by Light in a Similar but Not Identical Way as in Maize

In Vivo and in Vitro Phosphorylation of the Phosphoenolpyruvate Carboxylase from Wheat Seeds during Germination

Mitochondrial Redox State, Nitrogen Metabolism and Signalling

Contact Info

Product

Resources

About