Journal of Applied Biological Chemistry

The Korean Society for Applied Biological Chemistry (한국응용생명화학회)
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O-Methyltransferases from Arabidopsis thaliana

  • Kim, Bong-Gyu (Department of Molecular Biotechnology, Bio/Molecular Informatics Center, Konkuk University) ;
  • Kim, Dae-Hwan (Department of Molecular Biotechnology, Bio/Molecular Informatics Center, Konkuk University) ;
  • Hur, Hor-Gil (Department of Environmental Science and Engineering, Gwangju Institute of Science and Technology) ;
  • Lim, Jun (Department of Molecular Biotechnology, Bio/Molecular Informatics Center, Konkuk University) ;
  • Lim, Yoong-Ho (Department of Molecular Biotechnology, Bio/Molecular Informatics Center, Konkuk University) ;
  • Ahn, Joong-Hoon (Department of Molecular Biotechnology, Bio/Molecular Informatics Center, Konkuk University)
  • Published : 2005.09.30
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Abstract

O-methylation mediated by O-methyltransferases (OMTs) is a common modification in natural product biosynthesis and contributes to diversity of secondary metabolites. OMTs use phenylpropanoids, flavonoids, other phenolics and alkaloids as substrates, and share common domains for S-adenosyl-L-methionine (AdoMet) and substrate binding. We searched Arabiposis genome and found 17 OMTs genes (AtOMTs). AdoMet- and substrate-binding sites were predicted. AdoMet binding domain of AtOMTs is highly conserved, while substrate-binding domain is diverse, indicating use of different substrates. In addition, expressions of six AtOMT genes in response to UV and in different tissues were investigated using real-time quantitative reverse transcriptase-polymerase chain reaction. All the AtOMTs investigated were expressed under normal growth condition and most, except AtOMT10, were induced after UV illumination. AtOMT1 and AtOMT8 were expressed in all the tissues, whereas AtOMT10 showed flower-specific expression. Analysis of these AtOMT gene expressions could provide some clues on AtOMT involvement in the cellular processes.

Keywords

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