Reduction of Plant-Specific Arabinogalactan-Type O-Glycosylation by Treating Tobacco Plants with Ferrous Chelator 2,2′-Dipyridyl

Abstract

Plant specific O-glycosylation of proteins includes the attachment of arabinogalactan to hydroxyproline (Hyp) residues. These Hyp residues are generated from peptidyl proline residues by the action of prolyl 4-hydroxylase which requires the ferrous ion. We investigated the effect of the ferrous chelator, 2,2′-dipyridyl on tobacco plants, and found that such treatment reduced the arabinogalactosylation of proteins.

• arabinogalactan
• hydroxyproline
• prolyl 4-hydroxylase
• glycosylation
• plant