Nonspecific phospholipase <scp>C3</scp> of radish has phospholipase D activity towards glycosylinositol phosphoceramide

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  • Rumana Yesmin Hasi
    Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
  • Toshiki Ishikawa
    Graduate School of Science and Engineering Saitama University Japan
  • Keigo Sunagawa
    Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
  • Yoshimichi Takai
    Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
  • Hanif Ali
    Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
  • Junji Hayashi
    Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
  • Ryushi Kawakami
    Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
  • Keizo Yuasa
    Graduate School of Science and Engineering Setsunan University Neyagawa Japan
  • Mutsumi Aihara
    Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
  • Kaori Kanemaru
    Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan
  • Hiroyuki Imai
    Graduate School of Natural Science Konan University Kobe Japan
  • Tamotsu Tanaka
    Graduate School of Technology, Industrial and Social Sciences Tokushima University Japan

抄録

<jats:p>Glycosylinositol phosphoceramide (GIPC) is a major sphingolipid in the plasma membranes of plants. Previously, we found an enzyme activity that produces phytoceramide 1‐phosphate (PC1P) by hydrolysis of the D position of GIPC in cabbage and named this activity as GIPC‐phospholipase D (PLD). Here, we purified GIPC‐PLD by sequential chromatography from radish roots. Peptide mass fingerprinting analysis revealed that the potential candidate for GIPC‐PLD protein was nonspecific phospholipase C3 (NPC3), which has not been characterized as a PLD. The recombinant NPC3 protein obtained by heterologous expression system in <jats:italic>Escherichia coli</jats:italic> produced PC1P from GIPC and showed essentially the same enzymatic properties as those we characterized as GIPC‐PLD in cabbage, radish and <jats:italic>Arabidopsis thaliana.</jats:italic> From these results, we conclude that NPC3 is one of the enzymes that degrade GIPC.</jats:p>

収録刊行物

  • FEBS Letters

    FEBS Letters 596 (23), 3024-3036, 2022-10-31

    Wiley

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