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Acrolein-detoxifying isozymes of glutathione transferase in plants |
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| Authors: | Mano Jun’ichi Ishibashi Asami Muneuchi Hitoshi Morita Chihiro Sakai Hiroki Biswas Md. Sanaullah Koeduka Takao Kitajima Sakihito |
| Affiliation: | 1.Science Research Center, Organization for Research Initiatives, Yamaguchi University, Yoshida 1677-1, Yamaguchi, 753-8515, Japan ;2.Graduate School of Sciences and Technology for Innovation, Yamaguchi University, Yoshida 1677-1, Yamaguchi, 753-8515, Japan ;3.Graduate School of Agriculture, Yamaguchi University, Yoshida 1677-1, Yamaguchi, 753-8515, Japan ;4.Faculty of Agriculture, Yamaguchi University, Yoshida 1677-1, Yamaguchi, 753-8515, Japan ;5.The United Graduate School of Agriculture, Tottori University, Koyama-Cho Minami 4-101, Tottori, 680-8550, Japan ;6.Department of Horticulture, Bangabandhu Sheikh Mujibur Rahman Agricultural University, Gazipur, 1706, Bangladesh ;7.Department of Applied Biology, Kyoto Institute of Technology, Matsugasaki Sakyo-ku, Kyoto, 606-8585, Japan ;8.The Center for Advanced Insect Research Promotion, Kyoto Institute of Technology, Matsugasaki, Sakyo-ku, Kyoto, 606-8585, Japan ; |
| Abstract: | Main conclusion Acrolein is a lipid-derived highly reactive aldehyde, mediating oxidative signal and damage in plants. We found acrolein-scavenging glutathione transferase activity in plants and purified a low K M isozyme from spinach. Various environmental stressors on plants cause the generation of acrolein, a highly toxic aldehyde produced from lipid peroxides, via the promotion of the formation of reactive oxygen species, which oxidize membrane lipids. In mammals, acrolein is scavenged by glutathione transferase (GST; EC 2.5.1.18) isozymes of Alpha, Pi, and Mu classes, but plants lack these GST classes. We detected the acrolein-scavenging GST activity in four species of plants, and purified an isozyme showing this activity from spinach (Spinacia oleracea L.) leaves. The isozyme (GST-Acr), obtained after an affinity chromatography and two ion exchange chromatography steps, showed the K M value for acrolein 93 μM, the smallest value known for acrolein-detoxifying enzymes in plants. Peptide sequence homology search revealed that GST-Acr belongs to the GST Tau, a plant-specific class. The Arabidopsis thaliana GST Tau19, which has the closest sequence similar to spinach GST-Acr, also showed a high catalytic efficiency for acrolein. These results suggest that GST plays as a scavenger for acrolein in plants. |
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