Transformation of Arabidopsis with the codA gene for choline oxidase enhances freezing tolerance of plants

Sakamoto, Atsushi; Valverde, Roberto; Alia,; Chen, Tony H. H.; Murata, Norio

doi:10.1046/j.1365-313x.2000.00749.x

Cited by 116 publications

(59 citation statements)

References 24 publications

(21 reference statements)

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“…Second, CA, which is correlated with increased FT, is associated with GB accumulation (Naidu et al, 1991;Kishitani et al, 1994;Nomura et al, 1995;Allard et al, 1998). Third, exogenous applications of GB lead to significant increases in LT tolerance (Allard et al, 1998;Sakamoto et al, 2000).…”

Section: Table I In Vitro Phospho-base N-methyltransferase Activitiesmentioning

confidence: 99%

Molecular and Biochemical Characterization of a Cold-Regulated PhosphoethanolamineN-Methyltransferase from Wheat

et al. 2002

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A cDNA that encodes a methyltransferase (MT) was cloned from a cold-acclimated wheat (Triticum aestivum) cDNA library. Molecular analysis indicated that the enzyme WPEAMT (wheat phosphoethanolamine [P-EA] MT) is a bipartite protein with two separate sets of S-adenosyl-l-Met-binding domains, one close to the N-terminal end and the second close to the C-terminal end. The recombinant protein was found to catalyze the three sequential methylations of P-EA to form phosphocholine, a key precursor for the synthesis of phosphatidylcholine and glycine betaine in plants. Deletion and mutation analyses of the two S-adenosyl-l-Met-binding domains indicated that the N-terminal domain could perform the three N-methylation steps transforming P-EA to phosphocholine. This is in contrast to the MT from spinach (Spinacia oleracea), suggesting a different functional evolution for the monocot enzyme. The truncated C-terminal and the N-terminal mutated enzyme were only able to methylate phosphomonomethylethanolamine and phosphodimethylethanolamine, but not P-EA. This may suggest that the C-terminal part is involved in regulating the rate and the equilibrium of the three methylation steps. Northern and western analyses demonstrated that both Wpeamt transcript and the corresponding protein are up-regulated during cold acclimation. This accumulation was associated with an increase in enzyme activity, suggesting that the higher activity is due to de novo protein synthesis. The role of this enzyme during cold acclimation and the development of freezing tolerance are discussed.Winter survival and crop productivity are influenced by many different winter stresses, such as freezing temperature, length of freezing period, ice encasement, flooding, and oxidative stress caused by low temperature (LT)-induced photoinhibition (Fowler et al., 1999). Exposure of plants to LT produces morphological, physiological, and biochemical changes that are often highly correlated with plant freezing tolerance (FT) and winter survival. These changes are regulated by LT at the gene expression level. Cold-regulated genes and their products have been identified and characterized in many species (Thomashow, 1999). The complexity of the LT response has made it difficult to separate genes responsible for LT acclimation and cold hardiness from those associated with metabolic adjustments to LT. To characterize the genetic components associated with LT response, a better understanding of the LTresponsive genes responsible for adaptation to winter stresses and their interaction with the environment is needed (Fowler et al., 1999).

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Section: Table I In Vitro Phospho-base N-methyltransferase Activitiesmentioning

confidence: 99%

Molecular and Biochemical Characterization of a Cold-Regulated PhosphoethanolamineN-Methyltransferase from Wheat

et al. 2002

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“…The beneficial effects of seaweed extract application on crop performance have been attributed to a variety of constituents, including betaines (Blunden et al 1981). These naturally occurring quaternary ammonium compounds can act as osmolytes and/or affect gene expression, therefore improving plant tolerance to stresses such as temperature extremes, drought and salinity (Mason and Blunden 1989;Hayashi et al 1997;Holmström et al 2000;Sakamoto et al 2000;Park et al 2004;Yang et al 2007). …”

Section: Introductionmentioning

confidence: 99%

Improved methods of analysis for betaines in Ascophyllum nodosum and its commercial seaweed extracts

et al. 2009

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“…Model studies of Synechococcus sp. PCC 7942 or Arabidopsis thaliana transformed with the gene from A. globiformis that encodes choline oxidase, codA, have demonstrated an improved tolerance to salt stress (11) or high and freezing temperatures (2,16,40). Enhanced tolerance to low temperatures or high-salt conditions has been also observed during germination of transgenic seeds of A. thaliana transformed with codA (1,17).…”

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Cloning, Expression, and Purification of Choline Dehydrogenase from the Moderate Halophile Halomonas elongata

Gadda

Wilkins²

2003

Appl Environ Microbiol

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Choline dehydrogenase (EC 1.1.99.1) catalyzes the four-electron oxidation of choline to glycine-betaine via a betaine-aldehyde intermediate. Such a reaction is of considerable interest for biotechnological applications in that transgenic plants engineered with bacterial glycine-betaine-synthesizing enzymes have been shown to have enhanced tolerance towards various environmental stresses, such as hypersalinity, freezing, and high temperatures. To date, choline dehydrogenase has been poorly characterized in its biochemical and kinetic properties, mainly because its purification has been hampered by instability of the enzyme in vitro. In the present report, we cloned and expressed in Escherichia coli the betA gene from the moderate halophile Halomonas elongata which codes for a hypothetical choline dehydrogenase. The recombinant enzyme was purified to more than 70% homogeneity as judged by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and by treatment with 30 to 50% saturation of ammonium sulfate followed by column chromatography using DEAE-Sepharose. The purified enzyme showed similar substrate specificities with either choline or betainealdehyde as the substrate, as indicated by the apparent V/K values (where V is the maximal velocity and K is the Michaelis constant) of 0.9 and 0.6 mol of O 2 min ؊1 mg ؊1 mM ؊1 at pH 7 and 25°C, respectively. With 1 mM phenazine methosulfate as the primary electron acceptor, the apparent V max values for choline and betaine-aldehyde were 10.9 and 5.7 mol of O 2 min ؊1 mg ؊1 , respectively. These V max values decreased fourto sevenfold when molecular oxygen was used as the electron acceptor. Altogether, the kinetic data are consistent with the conclusion that H. elongata betA codes for a choline dehydrogenase that can also act as an oxidase when electron acceptors other than molecular oxygen are not available.

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Transformation of Arabidopsis with the codA gene for choline oxidase enhances freezing tolerance of plants

Cited by 116 publications

References 24 publications

Molecular and Biochemical Characterization of a Cold-Regulated PhosphoethanolamineN-Methyltransferase from Wheat

Molecular and Biochemical Characterization of a Cold-Regulated PhosphoethanolamineN-Methyltransferase from Wheat

Improved methods of analysis for betaines in Ascophyllum nodosum and its commercial seaweed extracts

Cloning, Expression, and Purification of Choline Dehydrogenase from the Moderate Halophile Halomonas elongata

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