Journal Article

Genetic engineering of glycinebetaine synthesis in plants: current status and implications for enhancement of stress tolerance

Atsushi Sakamoto and Norio Murata

in Journal of Experimental Botany

Volume 51, issue 342, pages 81-88
Published in print January 2000 | ISSN: 0022-0957
Published online January 2000 | e-ISSN: 1460-2431 | DOI: http://dx.doi.org/10.1093/jexbot/51.342.81
Genetic engineering of glycinebetaine synthesis in plants: current status and implications for enhancement of stress tolerance

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Metabolic acclimation via the accumulation of compatible solutes is regarded as a basic strategy for the protection and survival of plants in extreme environments. Certain plants accumulate significant amounts of glycinebetaine (betaine), a compatible quaternary amine, in response to high salinity, cold and drought. It is likely that betaine is involved in the protection of macrocomponents of plant cells, such as protein complexes and membranes, under stress conditions. Genetic engineering of the biosynthesis of betaine from choline has been the focus of considerable attention as a potential strategy for increasing stress tolerance in stress‐sensitive plants that are incapable of synthesizing this compatible/protective solute. Three distinct pathways for the synthesis of betaine have been identified in spinach, Escherichia coli and Arthrobacter globiformis, and various genes and cDNAs for the proteins involved are available. Moreover, each of the pathways has been exploited to a greater or lesser extent in efforts to convert betaine‐deficient plants to betaine accumulators. In this review, the potential of several recent examples of transgenic approaches to the enhancement of stress tolerance in plants is summarized and discussed.

Keywords: compatible solute; genetic engineering; glycinebetaine; stress tolerance; transgenic plants; BADH, betaine aldehyde dehydrogenase; betaine, glycinebetaine; CDH, choline dehydrogenase; CMO, choline monooxygenase; COD, choline oxidase; PSII, photosystem II; Rubisco, ribulose‐1,5‐bisphosphate carboxylase/oxygenase

Journal Article.  5140 words.  Illustrated.

Subjects: Plant Sciences and Forestry

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