Characterization of 5-Hydroxyconiferaldehyde <i>O</i>-Methyltransferase in <i>Oryza sativa</i>
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- Koshiba Taichi
- Research Institute for Sustainable Humanosphere, Kyoto University
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- Hirose Norie
- Research Institute for Sustainable Humanosphere, Kyoto University
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- Mukai Mai
- Research Institute for Sustainable Humanosphere, Kyoto University
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- Yamamura Masaomi
- Research Institute for Sustainable Humanosphere, Kyoto University
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- Hattori Takefumi
- Research Institute for Sustainable Humanosphere, Kyoto University
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- Suzuki Shiro
- Research Institute for Sustainable Humanosphere, Kyoto University
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- Sakamoto Masahiro
- Graduate School of Agriculture, Kyoto University
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- Umezawa Toshiaki
- Research Institute for Sustainable Humanosphere, Kyoto University Institute of Sustainability Science, Kyoto University
Bibliographic Information
- Other Title
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- Characterization of 5-Hydroxyconiferaldehyde O-Methyltransferase in Oryza sativa
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Abstract
Little is known regarding syringyl lignin biosynthesis in rice (Oryza sativa L. cv. Nipponbare). In the present study, the role of rice caffeic acid O-methyltransferase (OsCOMT1, Q6ZD89), was examined. The recombinant OsCOMT1 catalyzed the 5-Omethylation of 5-hydroxyferulate (5-HFA) and 5-hydroxyconiferaldehyde (5-HCAld). 5-HCAld inhibited 5-HFA methylation by this O-methyltransferase (OMT), while 5-HFA mitigated self-inhibition in 5-HCAld methylation. A rice plant in which OsCOMT1 expression was downregulated exhibited weakened cell wall staining with Wiesner reagent in vascular bundle cells and sclerenchyma tissue, compared with wild-type plants. The lignin content of transgenic rice plants was decreased and the syringyl lignin content reduced largely compared with that of the wild type. Taken together, these data indicated that OsCOMT1 functioned as a 5-HCAld OMT (OsCAldOMT1) in the biosynthetic pathway to syringyl lignin.
Journal
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- Plant Biotechnology
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Plant Biotechnology 30 (2), 157-167, 2013
Japanese Society for Plant Biotechnology
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Details 詳細情報について
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- CRID
- 1390001204327569152
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- NII Article ID
- 10031184120
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- NII Book ID
- AA11250821
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- COI
- 1:CAS:528:DC%2BC3sXhtlCqsL3L
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- ISSN
- 13476114
- 13424580
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- NDL BIB ID
- 024676595
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
- KAKEN
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- Abstract License Flag
- Disallowed