Plant Physiol.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 QUICK SEARCH:   [advanced]


     


Plant Physiology Preview
Published on February 13, 2003; 10.1104/pp.102.014639


This Article
Right arrow Full Text (Plant Physiology Preview (PDF))
Right arrow All Versions of this Article:
131/3/1250    most recent
pp.102.014639v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Web of Science (23)
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Pilon, M.
Right arrow Articles by Pilon-Smits, E. A.H.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Pilon, M.
Right arrow Articles by Pilon-Smits, E. A.H.
Agricola
Right arrow Articles by Pilon, M.
Right arrow Articles by Pilon-Smits, E. A.H.

Received September 13, 2002
Returned for revision October 10, 2002
Accepted November 27, 2002

Enhanced Selenium Tolerance and Accumulation in Transgenic Arabidopsis Expressing a Mouse Selenocysteine Lyase

Marinus Pilon , Jennifer D. Owen , Gulnara F. Garifullina , Tatsuo Kurihara , Hisaaki Mihara , Nobuyoshi Esaki , and Elizabeth A.H. Pilon-Smits *

Department of Biology, Colorado State University, Anatomy/Zoology Building, Fort Collins, Colorado 80523 (M.P., J.D.O., G.F.G., E.A.H.P.-S.); and Institute for Chemical Research, Kyoto University, Uji, Kyoto611-0011, Japan (T.K., H.M., N.E.)

* Corresponding author; email: epsmits{at}lamar.colostate.edu.

Selenium (Se) toxicity is thought to be due to nonspecific incorporation of selenocysteine (Se-Cys) into proteins, replacing Cys. In an attempt to direct Se flow away from incorporation into proteins, a mouse (Mus musculus) Se-Cys lyase (SL) was expressed in the cytosol or chloroplasts of Arabidopsis. This enzyme specifically catalyzes the decomposition of Se-Cys into elemental Se and alanine. The resulting SL transgenics were shown to express the mouse enzyme in the expected intracellular location, and to have SL activities up to 2-fold (cytosolic lines) or 6-fold (chloroplastic lines) higher than wild-type plants. Se incorporation into proteins was reduced 2-fold in both types of SL transgenics, indicating that the approach successfully redirected Se flow in the plant. Both the cytosolic and chloroplastic SL plants showed enhanced shoot Se concentrations, up to 1.5-fold compared with wild type. The cytosolic SL plants showed enhanced tolerance to Se, presumably because of their reduced protein Se levels. Surprisingly, the chloroplastic SL transgenics were less tolerant to Se, indicating that (over) production of elemental Se in the chloroplast is toxic. Expression of SL in the cytosol may be a useful approach for the creation of plants with enhanced Se phytoremediation capacity.




This article has been cited by other articles:


Home page
Plant Physiol.Home page
D. Van Hoewyk, G. F. Garifullina, A. R. Ackley, S. E. Abdel-Ghany, M. A. Marcus, S. Fakra, K. Ishiyama, E. Inoue, M. Pilon, H. Takahashi, et al.
Overexpression of AtCpNifS Enhances Selenium Tolerance and Accumulation in Arabidopsis
Plant Physiology, November 1, 2005; 139(3): 1518 - 1528.
[Abstract] [Full Text] [PDF]


Home page
Plant Physiol.Home page
P. V. Minorsky

Plant Physiology, September 1, 2003; 133(1): 14 - 15.
[Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 2003 by the American Society of Plant Biologists