The influence of plant pyruvate, orthophosphate dikinase on a C3 plant with respect to the intracellular location of the enzyme

Sheriff, A.; Meyer, H.; Riedel, E; Schmitt, Jürgen; Lapke, C.

doi:10.1016/s0168-9452(98)00090-9

Cited by 22 publications

(11 citation statements)

References 32 publications

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“…Support for a plastidial function of PPDK in regulating carbon flux into protein in C3 plants comes from studies of transgenic tobacco (Nicotiana tabacum; Sheriff et al, 1998). Plastidial PPDK from a Crassulacean acid metabolism plant was overexpressed either with or without its organelle-targeting peptide.…”

Section: Proposed Functional Associations In C670mentioning

confidence: 99%

Proteins from Multiple Metabolic Pathways Associate with Starch Biosynthetic Enzymes in High Molecular Weight Complexes: A Model for Regulation of Carbon Allocation in Maize Amyloplasts

et al. 2009

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Starch biosynthetic enzymes from maize (Zea mays) and wheat (Triticum aestivum) amyloplasts exist in cell extracts in high molecular weight complexes; however, the nature of those assemblies remains to be defined. This study tested the interdependence of the maize enzymes starch synthase IIa (SSIIa), SSIII, starch branching enzyme IIb (SBEIIb), and SBEIIa for assembly into multisubunit complexes. Mutations that eliminated any one of those proteins also prevented the others from assembling into a high molecular mass form of approximately 670 kD, so that SSIII, SSIIa, SBEIIa, and SBEIIb most likely all exist together in the same complex. SSIIa, SBEIIb, and SBEIIa, but not SSIII, were also interdependent for assembly into a complex of approximately 300 kD. SSIII, SSIIa, SBEIIa, and SBEIIb copurified through successive chromatography steps, and SBEIIa, SBEIIb, and SSIIa coimmunoprecipitated with SSIII in a phosphorylation-dependent manner. SBEIIa and SBEIIb also were retained on an affinity column bearing a specific conserved fragment of SSIII located outside of the SS catalytic domain. Additional proteins that copurified with SSIII in multiple biochemical methods included the two known isoforms of pyruvate orthophosphate dikinase (PPDK), large and small subunits of ADP-glucose pyrophosphorylase, and the sucrose synthase isoform SUS-SH1. PPDK and SUS-SH1 required SSIII, SSIIa, SBEIIa, and SBEIIb for assembly into the 670-kD complex. These complexes may function in global regulation of carbon partitioning between metabolic pathways in developing seeds.An important question in plant physiology is the means by which glucan storage homopolymers are synthesized such that they are able to assemble into semicrystalline starch granules. The starch polymer amylopectin consists of a-(1/4)-linked Glc units in linear chains, and these are joined to each other by a-(1/6) branch linkages. A distinguishing feature of amylopectin is that the branch points are clustered relative to each other (Thompson, 2000). The functional properties of starch depend on this ordered structure, which allows crystallization of the linear glucan chains that extend from the branch clusters. Packing of insoluble Glc units provides plants with a stable and abundant energy source to maintain metabolic needs in the absence of light. Considering that crystallization draws metabolic equilibria toward carbohydrate accumulation, another important physiological question is how the flux of reduced carbon is regulated such that seeds and other storage tissues achieve the proper balance of starch compared with protein and lipids.Biosynthesis of crystalline starch is accomplished in large part by the coordinated activities of starch synthases (SSs) and starch branching enzymes (SBEs), together with starch debranching enzymes (DBEs; Ball and Morell, 2003). SSs catalyze linear chain elongation by addition of a Glc unit donated from the nucleotide sugar ADP-Glc (ADPGlc) to the nonreducing end of an acceptor chain. Branch linkages are formed by the action of SBEs, whi...

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Section: Proposed Functional Associations In C670mentioning

confidence: 99%

Proteins from Multiple Metabolic Pathways Associate with Starch Biosynthetic Enzymes in High Molecular Weight Complexes: A Model for Regulation of Carbon Allocation in Maize Amyloplasts

et al. 2009

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“…In tobacco, it has been previously reported that the overexpression of the chloroplast-targeted M. crystallinum PPDK gene under the transcriptional control of the 35S promoter increased the number of seeds per seed capsule and the weight of each seed capsule by approximately 40% and 20%, respectively, with about a 1.5-fold increase in PPDK activity in leaves (Sheriff et al 1998). However, when the PPDK enzyme was expressed in the cytosol (by deleting the plastid signal sequence) under the transcriptional control of the 35S promoter, the transgenic tobacco plants produced less seeds than the wildtype and the transgenic line with the strongest phenotype produced nearly no seeds at all (Sheriff et al 1998). In contrast, the root-specific B33 promoter did not produce such a phenotype.…”

Section: Discussionmentioning

confidence: 98%

“…Several approaches have been carried out to overexpress PPDK in C 3 plants, including Arabidopsis (Ishimaru et al 1997;Voll et al 2003), potato (Ishimaru et al 1998), tobacco (Sheriff et al 1998) and rice (Nomura et al 2000;Fukayama et al 2001). In tobacco, it has been previously reported that the overexpression of the chloroplast-targeted M. crystallinum PPDK gene under the transcriptional control of the 35S promoter increased the number of seeds per seed capsule and the weight of each seed capsule by approximately 40% and 20%, respectively, with about a 1.5-fold increase in PPDK activity in leaves (Sheriff et al 1998).…”

Section: Discussionmentioning

confidence: 99%

“…Sequences of cDNAs encoding chloroplastic PPDK have been identified in other plant species ) but few of them possess cytosolic full length PPDK cDNAs (Agarie et al 1997). The facultative CAM plant Mesembryanthemum crystallinum contains a cDNA encoding plastidic PPDK (Fisslthaler et al 1995) that has been cloned into tobacco plants (Sheriff et al 1998) under the transcriptional control of the 35S promoter. PPDK has been reported to be involved in stress responses in various plant species (Fisslthaler et al 1995;Moons et al 1998).…”

Section: Introductionmentioning

confidence: 99%

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Transgenic tobacco plants overexpressing pyruvate phosphate dikinase increase exudation of organic acids and decrease accumulation of aluminum in the roots

et al. 2009

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Pyruvate phosphate dikinase (PPDK) catalyses the phosphorylation of pyruvate (+ ATP + Pi) yielding phosphoenolpyruvate (+ AMP + PPi). PPDK levels are induced upon drought and salt stress and both cytosolic and plastidic isoforms are found in higher plants. Herein we investigate the role of this enzyme upon aluminum exposure. We generated transgenic tobacco plants expressing either a plastidic (PPDK) or a putative cytosolic (ΔPPDK) Mesembryanthemum crystallinum PPDK under the transcriptional control of the patatin B33 promoter and found that they can ameliorate Al stress. Enhanced root growth in the presence of Al was observed in transgenic lines, while that of wild-type (WT) seedlings was strongly inhibited. Al content in root tips of stressed plants was reduced in the transgenic lines compared with WT, as judged by Eriochrome cyanine R (ECR) staining and atomic absorption spectrometry. Moreover, all transformants excreted higher levels of citric acid cycle intermediates (citrate and malate) than the WT seedlings did. Interestingly, we found different behavior between the two sets of transformants, based on results of ECR root staining, organic acid exudation and Al accumulation. In general, lines harboring the PPDK construct were more tolerant to Al stress than those expressing the ΔPPDK construct. We conclude that the overexpression of PPDK can serve to protect roots against Al toxicity. Furthermore, we provide the first physiological evidence for a link between Al stress and PPDK in plants and postulate that such approach could be successful under certain edaphic conditions, namely acid soils.

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“…For understanding the C3/CAM switch, the transfer of a CAM metabolism gene into C3 plants, for example the PPDK gene from M. crystallinum into tobacco was performed by Sheriff et al (1998) and Matsuoka et al (2001). Currently, a challenging research is being undertaken to try to change the carbon metabolism of some C3 crops into C4 photosynthesis to increase the yield, the most representative example being the attempt to obtain C4 rice (Doubnerova and Ryslava 2011).…”

Section: Introductionmentioning

confidence: 99%

The physiology of ex vitro pineapple (Ananas comosus L. Merr. var MD-2) as CAM or C3 is regulated by the environmental conditions

Aragón

Carvalho²,

González

et al. 2011

Plant Cell Rep

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Many plant species grown under in vitro controlled conditions can be used as models for the study of physiological processes. Adult pineapple can display CAM physiology while in vitro it functions as a C3 plant. Ex vitro Ananas comosus has plastic morphology and physiology, both easy to modify from C3 to CAM by changing the environmental conditions. The yield of survival for a rentable propagation protocol of pineapple is closely related with the C3/CAM shift and the associated physiological characteristics. In the present work, ex vitro pineapple plants were divided in two sets and subjected to C3 and CAM-inducing environmental conditions, determined by light intensity and relative humidity, respectively, 40 μmol m(-2) s(-1)/85% and 260 μmol m(-2) s(-1)/50%. The results demonstrated that the stress imposed by the environmental conditions switched pineapple plants from C3 to CAM behavior. Comparing to CAM induced, C3-induced pineapple plants showed substandard growth parameters and morphological leaf characteristics but a better rooting process and a higher ABA production, a phenotype closer to adult plants, which are expected to produce fruits in a normal production cycle. We conclude that the upholding of these characteristics is conditioned by low light intensity plus high relative humidity, especially during the first 8 weeks of ex vitro growth. It is expected that the better understanding of pineapple acclimatization will contribute to the design of a protocol to apply as a rentable tool in the pineapple agronomic industry.

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The influence of plant pyruvate, orthophosphate dikinase on a C3 plant with respect to the intracellular location of the enzyme

Cited by 22 publications

References 32 publications

Proteins from Multiple Metabolic Pathways Associate with Starch Biosynthetic Enzymes in High Molecular Weight Complexes: A Model for Regulation of Carbon Allocation in Maize Amyloplasts

Proteins from Multiple Metabolic Pathways Associate with Starch Biosynthetic Enzymes in High Molecular Weight Complexes: A Model for Regulation of Carbon Allocation in Maize Amyloplasts

Transgenic tobacco plants overexpressing pyruvate phosphate dikinase increase exudation of organic acids and decrease accumulation of aluminum in the roots

The physiology of ex vitro pineapple (Ananas comosus L. Merr. var MD-2) as CAM or C3 is regulated by the environmental conditions

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