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

Research output: Contribution to journalArticle

10 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 languageEnglish
Pages (from-to)994-996
Number of pages3
JournalBioscience, Biotechnology and Biochemistry
Volume75
Issue number5
DOIs
Publication statusPublished - Jun 6 2011

Fingerprint

Glycosylation
Tobacco
Hydroxyproline
Chelating Agents
Prolyl Hydroxylases
2,2'-Dipyridyl
Proline
Proteins
Ions
arabinogalactan

All Science Journal Classification (ASJC) codes

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

Cite this

Reduction of plant-specific arabinogalactan-type O-glycosylation by treating tobacco plants with ferrous chelator 2,20'-dipyridyl. / Moriguchi, Ryo; Matsuoka, Chiaya; Suyama, Akiko; Matsuoka, Ken.

In: Bioscience, Biotechnology and Biochemistry, Vol. 75, No. 5, 06.06.2011, p. 994-996.

Research output: Contribution to journalArticle

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