Plant Physiol. Journal of Pharmacology and Experimental Therapeutics
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Identification of a Functional Homolog of the Yeast Copper Homeostasis Gene ATX1 from Arabidopsis1

Edward Himelblau2, Helena Mira2, Su-Ju Lin, Valeria Cizewski Culotta, Lola Peñarrubia, and Richard M. Amasino*

Department of Biochemistry, University of Wisconsin, 420 Henry Mall, Madison, Wisconsin 53706 (E.H., R.M.A.); Departament de Bioquímica i Biologia Molecular, Universitat de València, Dr. Moliner 50, Burjassot, València, E-46100 Spain (H.M., L.P.); and Division of Toxicological Sciences, Department of Environmental Health Sciences, Johns Hopkins University School of Public Health, Bethesda, Maryland 20892 (S.-J.L., V.C.C.)

A cDNA clone encoding a homolog of the yeast (Saccharomyces cerevisiae) gene Anti-oxidant 1 (ATX1) has been identified from Arabidopsis. This gene, referred to as Copper CHaperone (CCH), encodes a protein that is 36% identical to the amino acid sequence of ATX1 and has a 48-amino acid extension at the C-terminal end, which is absent from ATX1 homologs identified in animals. ATX1-deficient yeast (atx1) displayed a loss of high-affinity iron uptake. Expression of CCH in the atx1 strain restored high-affinity iron uptake, demonstrating that CCH is a functional homolog of ATX1. When overexpressed in yeast lacking the superoxide dismutase gene SOD1, both ATX1 and CCH protected the cell from the reactive oxygen toxicity that results from superoxide dismutase deficiency. CCH was unable to rescue the sod1 phenotype in the absence of copper, indicating that CCH function is copper dependent. In Arabidopsis CCH mRNA is present in the root, leaf, and inflorescence and is up-regulated 7-fold in leaves undergoing senescence. In plants treated with 800 nL/L ozone for 30 min, CCH mRNA levels increased by 30%. In excised leaves and whole plants treated with high levels of exogenous CuSO4, CCH mRNA levels decreased, indicating that CCH is regulated differently than characterized metallothionein proteins in Arabidopsis.

1   E.H. and R.M.A. were supported by the Consortium for Plant Biotechnology Research (grant no. DE-FG02-97ER20280), E.H. was supported by the National Institutes of Health (NIH) Biotechnology Training Program (grant no. 5 T32 GM08349), H.M. and L.P. were supported by the Direccion General de Investigacion Cientifica y Technica Spain (grant no. PB95-0029-C02-02) and the Conselleria d' Educació y Ciencia de la Generalitat Valenciana, and S.-J.L. and V.C.C. were supported by the Johns Hopkins National Institute of Environmental Health Services Center and NIH (grant no. GM RO1 50016).
2   E.H. and H.M. contributed equally to the manuscript.
*   Corresponding author; e-mail amasino{at}biochem.wisc.edu; fax 1-608-262-3453.

Plant Physiol. (1998) 117: 1227-1234
Copyright Clearance Center:   0032-0889/98/117//08
© 1998 American Society of Plant Physiologists




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