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First published online April 2, 2004; 10.1104/pp.103.037614

Plant Physiology 134:1439-1449 (2004)
© 2004 American Society of Plant Biologists

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BIOCHEMICAL PROCESSES AND MACROMOLECULAR STRUCTURES

Arabidopsis CYP707As Encode (+)-Abscisic Acid 8'-Hydroxylase, a Key Enzyme in the Oxidative Catabolism of Abscisic Acid1

Shigeki Saito, Nobuhiro Hirai, Chiaki Matsumoto, Hajime Ohigashi, Daisaku Ohta, Kanzo Sakata and Masaharu Mizutani*

Institute for Chemical Research, Kyoto University, Uji, Kyoto 611–0011, Japan (S.S., K.S., M.M.); International Innovation Center, Kyoto University, Kyoto 606–8501, Japan (N.H.); Graduate School of Agriculture, Kyoto University, Kyoto 606–8502, Japan (C.M., H.O.); College of Agriculture, Osaka Prefecture University, Sakai, Osaka 599–8531, Japan (D.O.)

Abscisic acid (ABA) is involved in a number of critical processes in normal growth and development as well as in adaptive responses to environmental stresses. For correct and accurate actions, a physiologically active ABA level is controlled through fine-tuning of de novo biosynthesis and catabolism. The hydroxylation at the 8'-position of ABA is known as the key step of ABA catabolism, and this reaction is catalyzed by ABA 8'-hydroxylase, a cytochrome P450. Here, we demonstrate CYP707As as the P450 responsible for the 8'-hydroxylation of (+)-ABA. First, all four CYP707A cDNAs were cloned from Arabidopsis and used for the production of the recombinant proteins in insect cells using a baculovirus system. The insect cells expressing CYP707A3 efficiently metabolized (+)-ABA to yield phaseic acid, the isomerized form of 8'-hydroxy-ABA. The microsomes from the insect cells exhibited very strong activity of 8'-hydroxylation of (+)-ABA (Km = 1.3 µM and kcat = 15 min–1). The solubilized CYP707A3 protein bound (+)-ABA with the binding constant Ks = 3.5 µM, but did not bind (–)-ABA. Detailed analyses of the reaction products confirmed that CYP707A3 does not have the isomerization activity of 8'-hydroxy-ABA to phaseic acid. Further experiments revealed that Arabidopsis CYP707A1 and CYP707A4 also encode ABA 8'-hydroxylase. The transcripts of the CYP707A genes increased in response to salt, osmotic, and dehydration stresses as well as ABA. These results establish that the CYP707A family plays a key role in regulating the ABA level through the 8'-hydroxylation of (+)-ABA.

1 This work was supported by a part of the R&D Project of Industrial Science and Technology Frontier Program supported by NEDO (New Energy and Industrial Technology Development Organization), Japan (to D.O.).

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.103.037614.

* Corresponding author; e-mail mizutani{at}scl.kyoto-u.ac.jp; fax 81–774–38–3229.

Received December 12, 2003; returned for revision February 2, 2004; accepted February 6, 2004.




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