Reduction of plant-specific arabinogalactan-type O-glycosylation by treating tobacco plants with ferrous chelator 2,20'-dipyridyl

Ryo Moriguchi; Chiaya Matsuoka; Akiko Suyama; Ken Matsuoka

doi:10.1271/bbb.100884

Reduction of plant-specific arabinogalactan-type O-glycosylation by treating tobacco plants with ferrous chelator 2,20'-dipyridyl

Ryo Moriguchi, Chiaya Matsuoka, Akiko Suyama, Ken Matsuoka

Molecular Biosciences

Research output: Contribution to journal › Article › peer-review

11 Citations (Scopus)

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.

Original language	English
Pages (from-to)	994-996
Number of pages	3
Journal	Bioscience, Biotechnology and Biochemistry
Volume	75
Issue number	5
DOIs	https://doi.org/10.1271/bbb.100884
Publication status	Published - 2011

All Science Journal Classification (ASJC) codes

Biotechnology
Analytical Chemistry
Biochemistry
Applied Microbiology and Biotechnology
Molecular Biology
Organic Chemistry

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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.",

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AU - Matsuoka, Chiaya

AU - Suyama, Akiko

AU - Matsuoka, Ken

PY - 2011

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AB - 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.

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Reduction of plant-specific arabinogalactan-type O-glycosylation by treating tobacco plants with ferrous chelator 2,20'-dipyridyl

Abstract

All Science Journal Classification (ASJC) codes

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