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Reduction of plant-specific arabinogalactan-type O-glycosylation by treating tobacco plants with ferrous chelator 2,2'-dipyridyl.

Research paper by Ryo R Moriguchi, Chiaya C Matsuoka, Akiko A Suyama, Ken K Matsuoka

Indexed on: 21 May '11Published on: 21 May '11Published in: Bioscience, biotechnology, and biochemistry



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.