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

Hisashi Itô | Zendy; Masaki Iwabuchi | Zendy; Kenichi Ogawa | Zendy

Open Access

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

Author(s) -

Hisashi Itô,

Masaki Iwabuchi,

Kenichi Ogawa

Publication year - 2003

Publication title -

plant and cell physiology

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 1.975

H-Index - 152

eISSN - 1471-9053

pISSN - 0032-0781

DOI - 10.1093/pcp/pcg098

Subject(s) - aldolase a , biotinylation , biochemistry , glutathione , arabidopsis thaliana , arabidopsis , triosephosphate isomerase , enzyme , fructose bisphosphate aldolase , isomerase , biology , chemistry , mutant , gene

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.

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