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Plant and Cell Physiology 2004 45(9):1261-1270; doi:10.1093/pcp/pch150
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© 2004 Oxford University Press

Activation of Phospholipase D Induced by Hydrogen Peroxide in Suspension-cultured Rice Cells

Takeshi Yamaguchi1,4, Shigeru Tanabe2, Eiichi Minami2 and Naoto Shibuya3

1 Department of Rice Research, National Agricultural Research Center, National Agricultural and Bio-oriented Research Organization, Joetsu, Niigata, 943-0193 Japan
2 Biochemistry Department, National Institute of Agrobiological Sciences, Tsukuba, Ibaraki, 305-8602 Japan
3 Department of Life Sciences, Faculty of Agriculture, Meiji University, Kawasaki, Kanagawa, 214-8571 Japan

Hydrogen peroxide (H2O2) (10–100 µM) induced rapid and transient accumulation of phosphatidic acid (PA) in suspension-cultured rice cells. When phospholipase activity in the cellular extract fraction prepared from rice cells treated with H2O2 was assayed in the presence of 1-butanol (0.1%), rapid and transient phosphatidylbutanol (PtdBut) formation was observed. Thus, the H2O2-activated phospholipase was concluded to be phospholipase D (PLD). Furthermore, H2O2 directly induced in vitro PLD activation in the cytosolic fraction without H2O2 treatment. In vitro and in vivo activation of PLD were completely suppressed in the presence of lavendustin A (0.05 mM), a potent inhibitor of protein tyrosine kinase. Phytoalexin biosynthesis induced by N-acetylchitooligosaccharide elicitor was enhanced in the presence of H2O2 (10–100 µM), whereas it was suppressed in the presence of tiron, a potent scavenger of O2–, 1-butanol (0.1%) and lavendustin A (0.05 mM). These results indicate that H2O2-inducible PLD activation enhances signal transduction leading to phytoalexin biosynthesis in rice cells.

4 Corresponding author: E-mail : tkyama{at}affrc.go.jp; Fax, +81-25-524-8578.


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