Metabolism and physiological importance of L-arabinose in plants
| Project/Area Number |
16K07391
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| Research Category |
Grant-in-Aid for Scientific Research (C)
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| Allocation Type | Multi-year Fund |
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| Section | 一般 |
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| Research Field |
Plant molecular biology/Plant physiology
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| Research Institution | Saitama University |
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Principal Investigator |
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| Project Period (FY) |
2016-04-01 – 2019-03-31
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| Project Status |
Completed (Fiscal Year 2018)
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| Budget Amount *help |
¥4,940,000 (Direct Cost: ¥3,800,000、Indirect Cost: ¥1,140,000)
Fiscal Year 2018: ¥1,950,000 (Direct Cost: ¥1,500,000、Indirect Cost: ¥450,000)
Fiscal Year 2017: ¥1,430,000 (Direct Cost: ¥1,100,000、Indirect Cost: ¥330,000)
Fiscal Year 2016: ¥1,560,000 (Direct Cost: ¥1,200,000、Indirect Cost: ¥360,000)
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| Keywords | L-アラビノース / キシロース / 糖ヌクレオチド / シロイヌナズナ / 陸上植物 / UDP-グルコース4-エピメラーゼ / UDP-キシロース4-エピメラーゼ / UDP-L-アラビノース / 細胞壁多糖類 / 組換え酵素 / 細胞壁 / エピメラーゼ |
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| Outline of Final Research Achievements |
L-Arabinose (L-Ara) is a plant-specific sugar that is not found in animals. L-Ara is synthesized as a form of UDP-L-Ara from UDP-xylose (UDP-Xyl), which is catalyzed by UDP-glucose 4-epimease (UGE) 1 in the cytosol. Although UGE1 shares high similarity of amino acid sequence with UGE2, only UGE1 has UDP-Xyl 4-epimerae (UDP-L-Ara synthase) activity. To identify the amino acid residues important for UDP-L-Ara synthase activity, recombinant UGE1 proteins with a point mutation to replace a residue with that of UGE2 were prepared in E. coli. Three amino acid residues were found to affect UDP-L-Ara synthase activity of UGE1. To the contrary, mutated UGE2 with a residue corresponding to UGE1 showed weak UDP-L-Ara synthase activity. These results suggest that these residues have changed substrate specificity of UGE1, which enabled plants to synthesize UDP-L-Ara in the cytosol.
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| Academic Significance and Societal Importance of the Research Achievements |
L-アラビノースは動物にはない植物特有の糖であるが、植物がこの糖の合成系をどのように獲得したかはよくわかっていない。L-アラビノースの合成系は２経路あり、一つは細胞質基質に、もう一つはゴルジ体にある。このうち、前者の経路でL-アラビノース合成反応を行っている酵素について調べたところ、元々は別の働きを持っていた酵素が変異して、L-アラビノース合成も行うようになったことが示唆された。植物は２つのL-アラビノース合成系を獲得したことで、L-アラビノースの利用を加速させた可能性がある。
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Report
(4 results)
Research Products
(20 results)
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[Journal Article] A protease/peptidase from culture medium of Flammulina velutipes that acts on arabinogalactan-protein2017
Author(s)
Yoshimi, Y., Sugawara, Y., Hori, C., Igarashi, K., Kaneko, S., Tsumuraya, Y., and Kotake, T.
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Journal Title
Biosci. Biotechnol. Biochem.
Volume: 81
Issue: 3
Pages: 475-481
DOI
Related Report
Peer Reviewed
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[Presentation] KONJAC proteins affect glucomannan accumulation through the stimulation of GDP-mannose synthesis2016
Author(s)
Toshihisa Kotake, Shota Sawake, Noriaki Tajima, Jenny Mortimer, Lao Jeemeng, Toshiki Ishikawa, Xiaolan Yu, Yukiko Yamanashi, Yoshihisa Yoshimi, Maki Kawai-Yamada, Paul Dupree, Yoichi Tsumuraya
Organizer
Cell Wall Meeting
Place of Presentation
Minoa Palace（ギリシャ・クレタ島ハニア市）
Year and Date
2016-07-12
Related Report
Int'l Joint Research
