Phosphoenolpyruvate carboxylase: structure, regulation and evolution

Lepiniec, Loïc; Vidal, Jean; Chollet, Raymond; Gadal, Pierre; Crétin, Claude

doi:10.1016/0168-9452(94)90168-6

Cited by 160 publications

(152 citation statements)

References 112 publications

Supporting

Mentioning

148

Contrasting

Unclassified

Order By: Relevance

“…Therefore, these results extend the modulation effect of the APSIgG, previously shown for the recombinant Sorghum leaf C 4 PEPC , to the nonphotosynthetic isoforms from wheat seeds. The use of APS-lgGs with these crude extracts also provided a rapid and easy means to verify the enzyme's integrity with respect to the N-terminal phosphorylation domain and to argue that the N terminus of wheat seed PEPC is involved in the modification of its regulatory properties and catalytic activity, as described for other plant PEPCs (Echevarria et al, 1994;Lepiniec et al, 1994;Pacquit et al, 1995).…”

Section: The Effect Of Aps-igg On the Properties Of Seed Pepcmentioning

confidence: 99%

“…2B, lanes 2-4). This report documents that the wheat seed PEPC forms possess the consensus phosphorylation domain common to all plant PEPCs known so far (Sugimoto et al, 1992;Vazquez-Tello et al, 1993;Lepiniec et al, 1994). Despite the fact that a cocktail of proteinase inhibitors was included in the extraction buffer, proteolytic fragments were sometimes revealed by the specific polyclonal antibodies (Fig.…”

Section: Fragmentsmentioning

confidence: 99%

“…~~ PEPC (EC 4.1.1.31) is widely distributed in plants. A small multigene family encodes different forms of the enzyme that are involved in specific physiological functions (Lepiniec et al, 1994). A number of studies devoted to the photosynthetic PEPC from C, and CAM plants have shown that the enzyme is tightly regulated by light at both the transcriptional and posttranslational levels (Andreo et al, 1987;Leegood and Osmond, 1990;Huber et al, 1992;Nimmo, 1993;Gupta et al, 1994;Lepiniec et al, 1994;Rajagopalan et al, 1994).…”

mentioning

confidence: 99%

“…However, in none of these studies was the posttranslational regulation of seed PEPC examined. AI1 plant PEPCs sequenced so far, including C,, CAM, and C, species, have an N-terminal phosphorylation domain (Sugimoto et al, 1992;Vazquez-Tello et al, 1993;Lepiniec et al, 1994). The phosphorylation of a regulatory Ser in this domain impacts on the regulation of the enzyme by pH (Echevarría et al, 1994) and by opposing allosteric effectors, i.e.…”

mentioning

confidence: 99%

See 3 more Smart Citations

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

Section: The Effect Of Aps-igg On the Properties Of Seed Pepcmentioning

confidence: 99%

Section: Fragmentsmentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 2 more Smart Citations

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

show abstract

“…It is well established that PEPC in C, and CAM leaves is regulated by reversible protein phosphorylation and that this process in turn is controlled by a highly regulated protein-Ser/Thr kinase (Jiao and Chollet, 1991;Nimmo, 1993;Huber et al, 1994;Lepiniec et al, 1994). Two seemingly different scenarios exist for modulating the activity of PEPC-PK in C, and CAM leaves.…”

mentioning

confidence: 99%

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

Lyases

Mahdi¹,

Kelly²

2000

Biotechnology

View full text Add to dashboard Cite

Phosphoenolpyruvate carboxylase: structure, regulation and evolution

Cited by 160 publications

References 112 publications

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

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

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

Lyases

Contact Info

Product

Resources

About