Journal Article

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

Hisashi Ito, Masaki Iwabuchi and Ken’ichi Ogawa

in Plant and Cell Physiology

Published on behalf of Japanese Society of Plant Physiologists

Volume 44, issue 7, pages 655-660
Published in print July 2003 | ISSN: 0032-0781
Published online July 2003 | e-ISSN: 1471-9053 | DOI: http://dx.doi.org/10.1093/pcp/pcg098
The Sugar-Metabolic Enzymes Aldolase and Triose-Phosphate Isomerase are Targets of Glutathionylation in Arabidopsis thaliana: Detection using Biotinylated Glutathione

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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 GSSG, and it was reactivated by GSH. The physiological roles of glutathionylation of TPI and aldolase in sugar metabolism are discussed.

Keywords: Keywords: Aldorase — Arabidopsis thaliana — Glutathione — Glutathionylation — Redox regulation — Triose-phosphate isomerase.; Abbreviations: AMS, 4-acetamido-4′-maleimidylstilbene-2,2′-disulfonic acid; BioGEE, biotinylated GSH ethyl ester; BSA, bovine serum albumin; DTT, dithiothreitol; NEM, N-ethylmaleimide; TPI, triose-phosphate isomerase

Journal Article.  4854 words.  Illustrated.

Subjects: Biochemistry ; Molecular and Cell Biology ; Plant Sciences and Forestry

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