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Overexpression of ATP Sulfurylase in Indian Mustard Leads to Increased Selenate Uptake, Reduction, and Tolerance1

Elizabeth A.H. Pilon-Smits2, Seongbin Hwang, C. Mel Lytle, Yongliang Zhu, Jenny C. Tai, Rogelio C. Bravo, Yichang Chen, Tom Leustek, and Norman Terry*

Department of Plant and Microbial Biology, University of California, 111 Koshland Hall, Berkeley, California 94720 (E.A.H.P.-S., S.H., C.M.L., Y.Z., J.C.T., R.C.B., N.T.); and Center for Agricultural Molecular Biology, Rutgers University, 59 Dudley Road, New Brunswick, New Jersey 08901 (Y.C., T.L.)

In earlier studies, the assimilation of selenate by plants appeared to be limited by its reduction, a step that is thought to be mediated by ATP sulfurylase. Here, the Arabidopsis APS1 gene, encoding a plastidic ATP sulfurylase, was constitutively overexpressed in Indian mustard (Brassica juncea). Compared with that in untransformed plants, the ATP sulfurylase activity was 2- to 2.5-fold higher in shoots and roots of transgenic seedlings, and 1.5- to 2-fold higher in shoots but not roots of selenate-supplied mature ATP-sulfurylase-overexpressing (APS) plants. The APS plants showed increased selenate reduction: x-ray absorption spectroscopy showed that root and shoot tissues of mature APS plants contained mostly organic Se (possibly selenomethionine), whereas wild-type plants accumulated selenate. The APS plants were not able to reduce selenate when shoots were removed immediately before selenate was supplied. In addition, Se accumulation in APS plants was 2- to 3-fold higher in shoots and 1.5-fold higher in roots compared with wild-type plants, and Se tolerance was higher in both seedlings and mature APS plants. These studies show that ATP sulfurylase not only mediates selenate reduction in plants, but is also rate limiting for selenate uptake and assimilation.

1   This work was supported by Electric Power Research Institute grant no. W04163 to N.T., a TALENT stipend by the Dutch Organization for Scientific Research to E.A.H.P.-S., and Stanford Synchrotron Radiation Laboratory grant no. 2413 to C.M.L. and N.T.
2   Present address: Department of Biology, Colorado State University, A/Z Building, Fort Collins, CO 80523.
*   Corresponding author; e-mail nterry{at}nature.berkeley.edu; fax 1-510-642-3510.

Plant Physiol. (1999) 119: 123-132
Copyright Clearance Center:   0032-0889/99/119//10
© 1999 American Society of Plant Physiologists




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