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J. Biol. Chem., Vol. 281, Issue 36, 26280-26288, September 8, 2006

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AtGRXcp, an Arabidopsis Chloroplastic Glutaredoxin, Is Critical for Protection against Protein Oxidative Damage^*

Ning-Hui Cheng¹, Jian-Zhong Liu, Amanda Brock, Richard S. Nelson, and Kendal D. Hirschi^¶||

From the Plant Physiology Group, United States Department of Agriculture/Agricultural Research Service Children's Nutrition Research Center, Department of Pediatrics, Baylor College of Medicine, Houston, Texas 77030, Plant Biology Division, Samuel Roberts Noble Foundation, Inc., Ardmore, Oklahoma 73401, the ^¶Department of Molecular and Human Genetics, Baylor College of Medicine, Houston, Texas 77030, and the ^||Vegetable and Fruit Improvement Center, Texas A & M University, College Station, Texas 77845

Glutaredoxins (Grxs) are ubiquitous small heat-stable disulfide oxidoreductases and members of the thioredoxin (Trx) fold protein family. In bacterial, yeast, and mammalian cells, Grxs appear to be involved in maintaining cellular redox homeostasis. However, in plants, the physiological roles of Grxs have not been fully characterized. Recently, an emerging subgroup of Grxs with one cysteine residue in the putative active motif (monothiol Grxs) has been identified but not well characterized. Here we demonstrate that a plant protein, AtGRXcp, is a chloroplast-localized monothiol Grx with high similarity to yeast Grx5. In yeast expression assays, AtGRXcp localized to the mitochondria and suppressed the sensitivity of yeast grx5 cells to H₂O₂ and protein oxidation. AtGRXcp expression can also suppress iron accumulation and partially rescue the lysine auxotrophy of yeast grx5 cells. Analysis of the conserved monothiol motif suggests that the cysteine residue affects AtGRXcp expression and stability. In planta, AtGRXcp expression was elevated in young cotyledons, green tissues, and vascular bundles. Analysis of atgrxcp plants demonstrated defects in early seedling growth under oxidative stresses. In addition, atgrxcp lines displayed increased protein carbonylation within chloroplasts. Thus, this work describes the initial functional characterization of a plant monothiol Grx and suggests a conserved biological function in protecting cells against protein oxidative damage.

Received for publication, February 13, 2006 , and in revised form, June 16, 2006.

^* This work is supported by the United State Department of Agriculture/Agricultural Research Service under Cooperation Agreements 58-6250-6001K and 2004-34402-14768 and by National Science Foundation Grants 020977 and 0344350. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: Plant Physiology Group, USDA/ARS Children's Nutrition Research Center, Dept. of Pediatrics, Baylor College of Medicine, 1100 Bates St., Houston, TX 77030. Tel.: 713-798-7012; Fax: 713-798-7078; E-mail: ncheng{at}bcm.tmc.edu.

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