Plant-specific tau class glutathione transferases safeguard against lipid oxidation stress through dual detoxification of lipid peroxides and reactive carbonyl species
Yasuo YamauchiiD, Nagisa Matsuura, Fumiya Kawaguchi, Chisato Sakurai, Ryosuke Nakasuga, Junya ItoiD, Kiyotaka NakagawaiD, Masaharu MizutaniiD, Yukihiro SugimotoiD, Jun’ichi ManoiD
Abstract
O_LIOxidation of membrane lipids results in the formation of lipid peroxides (LOOHs) and reactive carbonyl species (RCS), that induce lipid oxidation stress in plants. The plant-specific tau class of glutathione transferases (GSTUs) possess both LOOH peroxidase and RCS-conjugating activities, but their overall contribution to stress tolerance remains unclear. C_LIO_LIWe systematically examined 16 GSTU isozymes of Arabidopsis thaliana and found that all catalysed glutathione-dependent reduction of LOOHs. GSTU17, showing the highest activity, recognized five different isomers of linoleic acid-derived hydroperoxides within comparable catalytic efficiencies. C_LIO_LIT-DNA mutants lacking GSTU3, GSTU17, GSTU18, GSTU19 or GSTU25--isoforms with strong conjugation activities toward acrolein, 4-hydroxynonenal or crotonal--displayed enhanced sensitivity to photooxidative stress, indicating that detoxification of RCS is crucial for oxidative protection. C_LIO_LITranscriptome analyses revealed that exposure to RCS (crotonal, 2-pentenal or 2-hexenal) strongly induced 12 GSTU genes, while other GST classes showed little response. Collectively, these results demonstrate that GSTUs function as a major enzymatic system mitigating lipid oxidation stress in A. thaliana through the combined detoxification of lipid peroxides and their reactive carbonyl products. C_LI
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