A lignan <i>O</i>-methyltransferase catalyzing the regioselective methylation of matairesinol in <i>Carthamus tinctorius</i>

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  • Umezawa Toshiaki
    Research Institute for Sustainable Humanosphere, Kyoto University Institute of Sustainability Science, Kyoto University
  • Ragamustari Safendrri Komara
    Research Institute for Sustainable Humanosphere, Kyoto University Institute of Sustainability Science, Kyoto University
  • Nakatsubo Tomoyuki
    Research Institute for Sustainable Humanosphere, Kyoto University
  • Wada Shohei
    Research Institute for Sustainable Humanosphere, Kyoto University
  • Li Laigeng
    Department of Forestry and Environmental Resources, College of Natural Resources, North Carolina State University Institute of Plant Physiology and Ecology, Shanghai Institute for Biological Sciences, Chinese Academy of Sciences
  • Yamamura Masaomi
    Research Institute for Sustainable Humanosphere, Kyoto University
  • Sakakibara Norikazu
    Research Institute for Sustainable Humanosphere, Kyoto University Faculty of Pharmaceutical Sciences at Kagawa Campus, Tokushima Bunri University
  • Hattori Takefumi
    Research Institute for Sustainable Humanosphere, Kyoto University Institute of Socio-Arts and Sciences, The University of Tokushima
  • Suzuki Shiro
    Research Institute for Sustainable Humanosphere, Kyoto University
  • Chiang Vincent L.
    Department of Forestry and Environmental Resources, College of Natural Resources, North Carolina State University

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  • A lignan O-methyltransferase catalyzing the regioselective methylation of matairesinol in Carthamus tinctorius

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Description

Lignans are a group of plant phenolic compounds with various biological activities, including antitumor and antioxidant properties. O-Methylation is a critical step in biosynthesis of these compounds. However, little is known about the O-methyltransferase (OMT) enzymes that catalyze lignan O-methylation. We discovered a highly regioselective OMT activity in safflower (Carthamus tinctorius) seeds that catalyzed the methylation of matairesinol, a dibenzylbutyrolactone lignan, into 4′-O-methylmatairesinol (arctigenin) but not 4-O-methylmatairesinol (isoarctigenin). By examining such OMT activity in correlation with OMT transcript abundances during seed development, we cloned a few putative OMT cDNAs and produced their recombinant proteins in Escherichia coli. Among them, one protein exhibited O-methylation activity for matairesinol with the regioselectivity identical to that of the plant protein, and was named C. tinctorius matairesinol OMT (CtMROMT). CtMROMT did not show any detectable OMT activities towards phenylpropanoid monomers under the reaction conditions tested, while it methylated flavonoid apigenin efficiently into 4′-O-methylapigenin (acacetin). However, quantitative real-time polymerase chain reaction analysis demonstrated that expression of the CtMROMT gene was synchronized with the CtMROMT activity profile and arctigenin accumulation in the plant. These results demonstrated that CtMROMT is a novel plant OMT for lignan methylation.

Journal

  • Plant Biotechnology

    Plant Biotechnology 30 (2), 97-109, 2013

    Japanese Society for Plant Biotechnology

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