Garifullina, Gulnara F., Owen, Jennifer D., Lindblom, Stormy Dawn, Tufan, Hale, Pilon, Marinus and Pilon-Smits, Elizabeth A.H. (2003) Expression of a mouse selenocysteine lyase in Brassica juncea chloroplasts affects selenium tolerance and accumulation. Physiologia Plantarum, 118 (4). pp. 538-544. ISSN 0031-9317 (Print), 1399-3054 (Online) (doi:10.1034/j.1399-3054.2003.00136.x)

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Abstract

Selenium is an essential nutrient for many organisms, as part of certain selenoproteins. However, selenium is toxic at high levels, which is thought to be due to non-specific replacement of cysteine by selenocysteine leading to disruption of protein function. In an attempt to prevent non-specific incorporation of selenocysteine into proteins and to possibly enhance plant selenium tolerance and accumulation, a mouse selenocysteine lyase was expressed in Brassica juncea (Indian mustard) chloroplasts, the site of selenocysteine synthesis. This selenocysteine lyase specifically breaks down selenocysteine into elemental selenium and alanine. The transgenic cpSL plants showed normal growth under standard conditions. Selenocysteine lyase activity in the cpSL transgenics was up to 6-fold higher than in wild-type plants. The cpSL transgenics contained up to 40% less selenium in protein compared to wild-type plants, indicating that Se flow in the plant was successfully redirected. Surprisingly, the selenium tolerance of the transgenic cpSL plants was reduced, perhaps due to interference of produced elemental selenium with chloroplastic sulphur metabolism. Shoot selenium levels were enhanced up to 50% in the cpSL transgenics, but only during the seedling stage.

Item Type:	Article
Additional Information:	[1] Journal published on behalf of Scandinavian Society for Plant Physiology.
Uncontrolled Keywords:	Indian mustard, Chlamydomonas-Reinhardtii, Selenoprotein synthesis, delivery protein, biosynthesis, plants, overexpression, volatilization, assimilation
Subjects:	S Agriculture > S Agriculture (General) S Agriculture > SB Plant culture
Faculty / School / Research Centre / Research Group:	Faculty of Engineering & Science > Natural Resources Institute
Related URLs:	Publisher
Last Modified:	17 Mar 2014 16:15
URI:	http://gala.gre.ac.uk/id/eprint/8210

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