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Plant and Cell Physiology, 2003, Vol. 44, No. 7 655-660
© 2003 Oxford University Press

The Sugar-Metabolic Enzymes Aldolase and Triose-Phosphate Isomerase are Targets of Glutathionylation in Arabidopsis thaliana: Detection using Biotinylated Glutathione

Hisashi Ito1,2, Masaki Iwabuchi1 and Ken’ichi Ogawa1,3,4

1 Research Institute for Biological Sciences, Okayama (RIBS Okayama), 7549-1 Yoshikawa, Kayou-cho, Okayama ,716-1241 Japan
2 The Japan Society for the Promotion of Science (JSPS), Kawaguchi, Saitama 332-0012, Japan
3 Core Research of Science and Technology (CREST), Japan Science and Technology Corporation (JST)

GSH has multiple actions in physiological responses of plants, but the molecular mechanisms are not fully understood. GSH plays an important role in functional alteration of proteins by reversible covalent incorporation (glutathionylation) in vertebrate cells. To investigate the function of glutathionylation in plant cells, we examined glutathionylated proteins in the suspension-cultured cells of Arabidopsis using biotinylated GSH. Biotinylated GSH was incorporated into about 20 proteins. Two of these proteins were identified as the key enzymes for sugar metabolism, triose-phosphate isomerase (TPI) and putative plastidic aldolase. Recombinant TPI was inactivated by GSSG, and it was reactivated by GSH. The physiological roles of glutathionylation of TPI and aldolase in sugar metabolism are discussed.

4 Corresponding author: E-mail, ogawa_k{at}bc4.so-net.ne.jp; Fax, +81-866-56-9454.


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