Proteome analysis of maize roots reveals that oxidative stress is a main contributing factor to plant arsenic toxicity.

Abstract To gain insight into plant responses to arsenic, the effect of arsenic exposure on maize ( Zea mays L.) root proteome has been examined. Maize seedlings were fed hydroponically with 300 μM sodium arsenate or 250 μM sodium arsenite for 24 h, and changes in differentially displayed proteins were studied by two-dimensional electrophoresis and digital image analysis. About 10% of total detected maize root proteins (67 out of 700) were up- or down-regulated by arsenic, among which 20 were selected as being quite reproducibly affected by the metalloid. These were analyzed by matrix-assisted laser desorption/ionization-time of flight mass spectrometry and 11 of them could be identified by comparing their peptide mass fingerprints against protein- and expressed sequence tag-databases. The set of identified maize root proteins highly responsive to arsenic exposure included a major and functionally homogeneous group of seven enzymes involved in cellular homeostasis for redox perturbation (e.g., three superoxide dismutases, two glutathione peroxidases, one peroxiredoxin, and one p -benzoquinone reductase) besides four additional, functionally heterogeneous, proteins (e.g., ATP synthase, succinyl-CoA synthetase, cytochrome P450 and guanine nucleotide-binding protein β subunit). These findings strongly suggest that the induction of oxidative stress is a main process underlying arsenic toxicity in plants.