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

Choline oxidase, isolated from the soil bacterium Arthrobacter globiformis, converts choline to glycine-betaine (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 c...

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Bibliographic Details
Published in:Plant molecular biology Vol. 29; no. 5; pp. 897 - 907
Main Authors: Deshnium, P, Los, D.A, Hayashi, H, Mustardy, L, Murata, N
Format: Journal Article
Language:English
Published: Netherlands 01-12-1995
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Summary:Choline oxidase, isolated from the soil bacterium Arthrobacter globiformis, converts choline to glycine-betaine (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 glycine-betaine 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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ISSN:0167-4412
1573-5028
DOI:10.1007/BF00014964