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First published online October 15, 2004; 10.1104/pp.104.046672 Plant Physiology 136:3824-3837 (2004) © 2004 American Society of Plant Biologists Cesium Toxicity in Arabidopsis1Warwick HRI, Warwick CV35 9EF, United Kingdom (C.R.H., H.C.B., J.P.H., A.M., K.A.P., P.J.W.); School of Biological Sciences, The University of Birmingham, Birmingham B15 2TT, United Kingdom (C.R.H., J.P.); and Plant Sciences Division, University of Nottingham, Sutton Bonington Campus, Loughborough LE12 5RD, United Kingdom (M.R.B., J.P.H., K.A.P.)
Cesium (Cs) is chemically similar to potassium (K). However, although K is an essential element, Cs is toxic to plants. Two contrasting hypotheses to explain Cs toxicity have been proposed: (1) extracellular Cs+ prevents K+ uptake and, thereby, induces K starvation; and (2) intracellular Cs+ interacts with vital K+-binding sites in proteins, either competitively or noncompetitively, impairing their activities. We tested these hypotheses with Arabidopsis (Arabidopsis thaliana). Increasing the Cs concentration in the agar ([Cs]agar) on which Arabidopsis were grown reduced shoot growth. Increasing the K concentration in the agar ([K]agar) increased the [Cs]agar at which Cs toxicity was observed. However, although increasing [Cs]agar reduced shoot K concentration ([K]shoot), the decrease in shoot growth appeared unrelated to [K]shoot per se. Furthermore, the changes in gene expression in Cs-intoxicated plants differed from those of K-starved plants, suggesting that Cs intoxication was not perceived genetically solely as K starvation. In addition to reducing [K]shoot, increasing [Cs]agar also increased shoot Cs concentration ([Cs]shoot), but shoot growth appeared unrelated to [Cs]shoot per se. The relationship between shoot growth and [Cs]shoot/[K]shoot suggested that, at a nontoxic [Cs]shoot, growth was determined by [K]shoot but that the growth of Cs-intoxicated plants was related to the [Cs]shoot/[K]shoot quotient. This is consistent with Cs intoxication resulting from competition between K+ and Cs+ for K+-binding sites on essential proteins.
1 This work was supported by the Biotechnology and Biological Sciences Research Council (UK). C.R.H. was supported by an HRI/Birmingham University Studentship, J.P.H. was supported by an HRI Browning Studentship, and K.A.P. was supported by a BBSRC Committee Studentship. Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.104.046672. * Corresponding author; e-mail philip-j.white{at}warwick.ac.uk; fax 44(0)2476574500. Received May 19, 2004; returned for revision May 30, 2004; accepted May 30, 2004. This article has been cited by other articles:
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