Plant Mol Biol. 1995 Dec;29(5):897-907.

Transformation of Synechococcus with a gene for choline oxidase enhances tolerance to salt stress.

Deshnium P, Los DA, Hayashi H, Mustardy L, Murata N.

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Department of Regulation Biology, National Institute for Basic Biology, Okazaki, Japan.

Abstract

Choline oxidase, isolated from the soil bacterium Arthrobacter globiformis, converts choline to glycinebetaine (N-trimethylglycine) without a requirement for any cofactors. The gene for this enzyme, designated codA, was cloned and introduced into the cyanobacterium Synechococcus sp. PCC 7942. The codA gene was expressed under the control of a strong constitutive promoter, and the transformed cells accumulated glycinebetaine at intracellular levels of 60-80 mM. Consequently the cells acquired tolerance to salt stress, as evaluated in terms of growth, accumulation of chlorophyll and photosynthetic activity.

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Transformation of Arabidopsis thaliana with the codA gene for choline oxidase; accumulation of glycinebetaine and enhanced tolerance to salt and cold stress. [Plant J. 1997]
Transformation of Arabidopsis thaliana with the codA gene for choline oxidase; accumulation of glycinebetaine and enhanced tolerance to salt and cold stress.
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Cited by 11 PubMed Central articles

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Billini M, Stamatakis K, Sophianopoulou V. J Bacteriol. 2008 Oct; 190(19):6318-29. Epub 2008 Jul 18.
Glycinebetaine counteracts the inhibitory effects of salt stress on the degradation and synthesis of D1 protein during photoinhibition in Synechococcus sp. PCC 7942. [Plant Physiol. 2006]
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Transformation of Synechococcus with a gene for choline oxidase enhances tolerance to salt stress.
Plant Mol Biol. 1995 Dec ;29(5):897-907.

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