期刊
PLANT AND CELL PHYSIOLOGY
卷 45, 期 9, 页码 1261-1270出版社
OXFORD UNIV PRESS
DOI: 10.1093/pcp/pch150
关键词
hydrogen peroxide; phospholipase D; phytoalexin; protein tyrosine kinase
Hydrogen peroxide (H2O2) (10-100 muM) 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 muM), whereas it was suppressed in the presence of tiron, a potent scavenger of O-2(-), 1-butanol (0.1%) and lavendustin A (0.05mM). These results indicate that H2O2-inducible PLD activation enhances signal transduction leading to phytoalexin biosynthesis in rice cells.
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