Overexpression of C(4)-cycle enzymes in transgenic C(3) plants : a biotechnological approach to improve C(3)-photosynthesis

The process of photorespiration diminishes the efficiency of CO(2) assimilation and yield of C(3)-crops such as wheat, rice, soybean or potato, which are important for feeding the growing world population. Photorespiration starts with the competitive inhibition of CO(2) fixation by O(2) at the activ...

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Veröffentlicht in:Journal of experimental botany. - 1985. - 53(2002), 369 vom: 31. Apr., Seite 591-607
1. Verfasser: Häusler, Rainer E (VerfasserIn)
Weitere Verfasser: Hirsch, Heinz-Josef, Kreuzaler, Fritz, Peterhänsel, Christoph
Format: Aufsatz
Sprache:English
Veröffentlicht: 2002
Zugriff auf das übergeordnete Werk:Journal of experimental botany
Schlagworte:Journal Article Review Enzymes Photosynthetic Reaction Center Complex Proteins Plant Proteins Carbon Dioxide 142M471B3J Malate Dehydrogenase EC 1.1.1.37 malate dehydrogenase-(oxaloacetate-decarboxylating) (NAD+) mehr... EC 1.1.1.38 malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+) EC 1.1.1.40 phosphoenolpyruvate carboxylase kinase EC 2.7.1.- Protein Serine-Threonine Kinases EC 2.7.11.1 PPDK protein, Zea mays EC 2.7.9.1 Pyruvate, Orthophosphate Dikinase Phosphoenolpyruvate Carboxylase EC 4.1.1.31 Ribulose-Bisphosphate Carboxylase EC 4.1.1.39 Carbonic Anhydrases EC 4.2.1.1 Oxygen S88TT14065
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100 1 |a Häusler, Rainer E  |e verfasserin  |4 aut 
245 1 0 |a Overexpression of C(4)-cycle enzymes in transgenic C(3) plants  |b a biotechnological approach to improve C(3)-photosynthesis 
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520 |a The process of photorespiration diminishes the efficiency of CO(2) assimilation and yield of C(3)-crops such as wheat, rice, soybean or potato, which are important for feeding the growing world population. Photorespiration starts with the competitive inhibition of CO(2) fixation by O(2) at the active site of ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco) and can result in a loss of up to 50% of the CO(2) fixed in ambient air. By contrast, C(4) plants, such as maize, sugar cane and Sorghum, possess a CO(2) concentrating mechanism, by which atmospheric CO(2) is bound to C(4)-carbon compounds and shuttled from the mesophyll cells where the prefixation of bicarbonate occurs via phosphoenolpyruvate carboxylase (PEPC) into the gas-tight bundle-sheath cells, where the bound carbon is released again as CO(2) and enters the Calvin cycle. However, the anatomical division into mesophyll and bundle-sheaths cells ("Kranz"-anatomy) appears not to be a prerequisite for the operation of a CO(2) concentrating mechanism. Submerged aquatic macrophytes, for instance, can induce a C(4)-like CO(2) concentrating mechanism in only one cell type when CO(2) becomes limiting. A single cell C(4)-mechanism has also been reported recently for a terrestrial chenopod. For over 10 years researchers in laboratories around the world have attempted to improve photosynthesis and crop yield by introducing a single cell C(4)-cycle in C(3) plants by a transgenic approach. In the meantime, there has been substantial progress in overexpressing the key enzymes of the C(4) cycle in rice, potato, and tobacco. In this review there will be a focus on biochemical and physiological consequences of the overexpression of C(4)-cycle genes in C(3) plants. Bearing in mind that C(4)-cycle enzymes are also present in C(3) plants, the pitfalls encountered when C(3) metabolism is perturbed by the overexpression of individual C(4) genes will also be discussed 
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650 4 |a Review 
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650 7 |a Photosynthetic Reaction Center Complex Proteins  |2 NLM 
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650 7 |a Carbon Dioxide  |2 NLM 
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650 7 |a malate dehydrogenase (oxaloacetate-decarboxylating) (NADP+)  |2 NLM 
650 7 |a EC 1.1.1.40  |2 NLM 
650 7 |a phosphoenolpyruvate carboxylase kinase  |2 NLM 
650 7 |a EC 2.7.1.-  |2 NLM 
650 7 |a Protein Serine-Threonine Kinases  |2 NLM 
650 7 |a EC 2.7.11.1  |2 NLM 
650 7 |a PPDK protein, Zea mays  |2 NLM 
650 7 |a EC 2.7.9.1  |2 NLM 
650 7 |a Pyruvate, Orthophosphate Dikinase  |2 NLM 
650 7 |a EC 2.7.9.1  |2 NLM 
650 7 |a Phosphoenolpyruvate Carboxylase  |2 NLM 
650 7 |a EC 4.1.1.31  |2 NLM 
650 7 |a Ribulose-Bisphosphate Carboxylase  |2 NLM 
650 7 |a EC 4.1.1.39  |2 NLM 
650 7 |a Carbonic Anhydrases  |2 NLM 
650 7 |a EC 4.2.1.1  |2 NLM 
650 7 |a Oxygen  |2 NLM 
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700 1 |a Hirsch, Heinz-Josef  |e verfasserin  |4 aut 
700 1 |a Kreuzaler, Fritz  |e verfasserin  |4 aut 
700 1 |a Peterhänsel, Christoph  |e verfasserin  |4 aut 
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