Journal
PLANT AND CELL PHYSIOLOGY
Volume 44, Issue 7, Pages 655-660Publisher
OXFORD UNIV PRESS
DOI: 10.1093/pcp/pcg098
Keywords
aldorase; Arabidopsis thaliana; glutathione; glutathionylation; redox regulation; triose-phosphate isomerase
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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 GSSC and it was reactivated by GSH. The physiological roles of glutathionylation of TPI and aldolase in sugar metabolism are discussed.
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