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

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概要

• 論文の詳細を見る

• 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.

• 社団法人 日本農芸化学会の論文
• 2011-05-23

著者

• Matsuoka Ken

  Laboratory Of Biochemistry Faculty Of Agriculture Nagoya University

• MORIGUCHI Ryo

  Laboratory of Plant Nutrition, Faculty of Agriculture, Kyushu University

• MATSUOKA Chiaya

  Laboratory of Plant Nutrition, School of Agriculture, Kyushu University

• SUYAMA Akiko

  Laboratory of Plant Nutrition, Faculty of Agriculture, Kyushu University

• Suyama Akiko

  Laboratory Of Plant Nutrition Faculty Of Agriculture Kyushu University

• Moriguchi Ryo

  Laboratory Of Plant Nutrition Faculty Of Agriculture Kyushu University

• Matsuoka Chiaya

  Laboratory Of Plant Nutrition School Of Agriculture Kyushu University

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• Transport of a Sweet Potato Storage Protein, Sporamin, to the Vacuole in Yeast Cells
• A Major Jasmonate-Inducible Protein of Sweet Potato, Ipomoelin, is an ABA-Independent Wound-Inducible Protein
• The N-Terminal Propeptide and the C Terminus of the Precursor to 20-kilo-dalton Potato Tuber Protein Can Function as Different Types of Vacuolar Sorting Signals
• Closing Plant Stomata Requires a Homolog of an Aluminum-Activated Malate Transporter
• Reduction of Plant-Specific Arabinogalactan-Type O-Glycosylation by Treating Tobacco Plants with Ferrous Chelator 2,2'-Dipyridyl
• Role of Lumenal Domain on Intracellular Localization of Tobacco Membrane-Anchored Prolyl 4-Hydroxylase

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