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https://hdl.handle.net/2440/47037
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dc.contributor.author | Ellis, D. | - |
dc.contributor.author | Sors, T. | - |
dc.contributor.author | Brunk, D. | - |
dc.contributor.author | Albrecht, C. | - |
dc.contributor.author | Orser, C. | - |
dc.contributor.author | Lahner, B. | - |
dc.contributor.author | Wood, K. | - |
dc.contributor.author | Harris, H. | - |
dc.contributor.author | Pickering, I. | - |
dc.contributor.author | Salt, D. | - |
dc.date.issued | 2004 | - |
dc.identifier.citation | BMC Plant Biology, 2004; 4(28):Artilcle 1- | - |
dc.identifier.issn | 1471-2229 | - |
dc.identifier.issn | 1471-2229 | - |
dc.identifier.uri | http://hdl.handle.net/2440/47037 | - |
dc.description.abstract | Background: It has become increasingly evident that dietary Se plays a significant role in reducing the incidence of lung, colorectal and prostate cancer in humans. Different forms of Se vary in their chemopreventative efficacy, with Se-methylselenocysteine being one of the most potent. Interestingly, the Se accumulating plant Astragalus bisulcatus (Two-grooved poison vetch) contains up to 0.6% of its shoot dry weight as Se-methylselenocysteine. The ability of this Se accumulator to biosynthesize Se-methylselenocysteine provides a critical metabolic shunt that prevents selenocysteine and selenomethionine from entering the protein biosynthetic machinery. Such a metabolic shunt has been proposed to be vital for Se tolerance in A. bisulcatus. Utilization of this mechanism in other plants may provide a possible avenue for the genetic engineering of Se tolerance in plants ideally suited for the phytoremediation of Se contaminated land. Here, we describe the overexpression of a selenocysteine methyltransferase from A. bisulcatus to engineer Se-methylselenocysteine metabolism in the Se non-accumulator Arabidopsis thaliana (Thale cress). Results: By over producing the A. bisulcatus enzyme selenocysteine methyltransferase in A. thaliana, we have introduced a novel biosynthetic ability that allows the non-accumulator to accumulate Se-methylselenocysteine and γ-glutamylmethylselenocysteine in shoots. The biosynthesis of Se-methylselenocysteine in A. thaliana also confers significantly increased selenite tolerance and foliar Se accumulation. Conclusion: These results demonstrate the feasibility of developing transgenic plant-based production of Se-methylselenocysteine, as well as bioengineering selenite resistance in plants. Selenite resistance is the first step in engineering plants that are resistant to selenate, the predominant form of Se in the environment. | - |
dc.description.statementofresponsibility | Danielle R Ellis, Thomas G Sors, Dennis G Brunk, Carrie Albrecht, Cindy Orser, Brett Lahner, Karl V Wood, Hugh H Harris, Ingrid J Pickering and David E Salt | - |
dc.language.iso | en | - |
dc.publisher | BioMed Central Ltd. | - |
dc.rights | Copyright © 2004 Ellis et al; licensee BioMed Central Ltd. | - |
dc.source.uri | http://www.biomedcentral.com/1471-2229/4/1 | - |
dc.subject | Plants, Genetically Modified | - |
dc.subject | Arabidopsis | - |
dc.subject | Astragalus Plant | - |
dc.subject | Plant Shoots | - |
dc.subject | Selenium | - |
dc.subject | Sodium Selenite | - |
dc.subject | Organoselenium Compounds | - |
dc.subject | Selenocysteine | - |
dc.subject | Cysteine | - |
dc.subject | Methyltransferases | - |
dc.subject | Chromatography, High Pressure Liquid | - |
dc.subject | Gene Expression Regulation, Enzymologic | - |
dc.subject | Gene Expression Regulation, Plant | - |
dc.subject | Mass Spectrometry | - |
dc.title | Production of Se-methylselenocysteine in transgenic plants expressing selenocysteine methyltransferase | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1186/1471-2229-4-1 | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Harris, H. [0000-0002-3472-8628] | - |
Appears in Collections: | Aurora harvest 6 Chemistry and Physics publications Environment Institute publications |
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hdl_47037.pdf | Published version | 530 kB | Adobe PDF | View/Open |
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