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Allene oxide cyclase is essential for theobroxide-induced jasmonic acid biosynthesis in Pharbitis nil

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Title: Allene oxide cyclase is essential for theobroxide-induced jasmonic acid biosynthesis in Pharbitis nil
Authors: Kong, Fanjiang Browse this author
Abe, Jun Browse this author →KAKEN DB
Takahashi, Kosaku Browse this author →KAKEN DB
Matsuura, Hideyuki Browse this author
Yoshihara, Teruhiko Browse this author
Nabeta, Kensuke Browse this author
Keywords: Allene oxide cyclase
Allene oxide synthase
Jasmonic acid
Lipoxygenase
Pharbitis nil
Theobroxide
Issue Date: 4-Nov-2005
Publisher: Elsevier
Journal Title: Biochemical and Biophysical Research Communications
Volume: 336
Issue: 4
Start Page: 1150
End Page: 1156
Publisher DOI: 10.1016/j.bbrc.2005.08.246
PMID: 16168955
Abstract: Theobroxide, a natural product, strongly stimulates the biosynthesis of jasmonic acid (JA) in Pharbitis nil. In this study, we investigated the accumulation of protein by the immunoblot analysis of lipoxygenase (LOX), allene oxide synthase (AOS) and allene oxide cyclase (AOC), key enzymes in JA biosynthesis, and how the endogenous levels of JA in Pharbitis nil are affected by theobroxide. The effect of JA on the accumulations of these proteins was monitored simultaneously. The results show that theobroxide treatment led to a high level accumulation of JA, which is due to high accumulations of LOX, AOS and AOC proteins induced by theobroxide treatment both under short day (SD) and long day (LD) conditions. However, under SD conditions AOS and AOC proteins are not enhanced by JA treatment. Kinetic analysis of protein levels show that a biphasic activation of AOC protein by theobroxide is displayed and the first activation of AOC protein together with elevated JA levels are observed within 30 minutes after treatment. Meanwhile, AOS and LOX proteins are activated by theobroxide later than AOC protein, suggesting that AOC plays an essential role in the initial JA formation induced by theobroxide. Since theobroxide-increased JA levels also show a biphasic manner similar to AOC activation and AOS, LOX proteins are activated later than AOC, and thus we propose a positive JA feedback regulation. Interestingly, AOS protein, which is also the enzyme for the biosynthesis of 9,10-ketol-octadecadienoic acid (KODA, a flowering inducing factor), accumulates markedly due to the simultaneous involvement of theobroxide and SD conditions, suggesting that AOS probably plays a role in flower bud formation in Pharbitis nil.
Rights: Copyright © 2006 Elsevier GmbH. All rights reserved
Relation: http://www.sciencedirect.com/science/journal/0006291X
Type: article (author version)
URI: http://hdl.handle.net/2115/8514
Appears in Collections:農学院・農学研究院 (Graduate School of Agriculture / Faculty of Agriculture) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: Fanjiang Kong

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