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Plant Physiol, June 2001, Vol. 126, pp. 770-779

Brassinosteroid-6-Oxidases from Arabidopsis and Tomato Catalyze Multiple C-6 Oxidations in Brassinosteroid Biosynthesis1

Yukihisa Shimada,* Shozo Fujioka, Narumasa Miyauchi, Masayo Kushiro, Suguru Takatsuto, Takahito Nomura, Takao Yokota, Yuji Kamiya, Gerard J. Bishop, and Shigeo Yoshida

Plant Science Center, RIKEN, Wako-shi, Saitama 351-0198, Japan (Y.S., S.F., N.M., M.K., Y.K., S.Y.); Laboratory of Nutrition Biochemistry, National Food Research Institute, Ministry of Agriculture, Forestry, and Fisheries, 2-1-2 Kannondai, Tsukuba, Ibaraki 305-8642, Japan (M.K.); Department of Chemistry, Joetsu University of Education, Joetsu-shi, Niigata 943-8512, Japan (S.T.); Department of Biosciences, Teikyo University, Utsunomiya 320-8551, Japan (T.N., T.Y.); and Institute of Biological Sciences, The University of Wales, Cledwyn Building, Aberystwyth, Ceredigion SY23 3DD, United Kingdom (G.J.B.)

Brassinosteroids (BRs) are steroidal plant hormones that are essential for growth and development. It has been proposed that BRs are synthesized via two parallel pathways, the early and late C-6 oxidation pathways according to the C-6 oxidation status. The tomato (Lycopersicon esculentum) Dwarf gene encodes a cytochrome P450 that has been shown to catalyze the C-6 oxidation of 6-deoxocastasterone to castasterone. We isolated an Arabidopsis ortholog (AtBR6ox gene) of the tomato Dwarf gene. The encoded polypeptide has characteristics of P450s and is classified into the CYP85 family. The AtBR6ox and tomato Dwarf gene were expressed in yeast and the ability of the transformed yeast cells to metabolize 6-deoxo-BRs was tested. Metabolites were analyzed by gas chromatography-mass spectrometry. Both enzymes catalyze multiple steps in BR biosynthesis: 6-deoxoteasterone to teasterone, 3-dehydro-6-deoxoteasterone to 3-dehydroteasterone, 6-deoxotyphasterol to typhasterol, and 6-deoxocastasterone to castasterone. Our results indicate that the AtBR6ox gene and the tomato Dwarf gene encode steroid-6-oxidases and that these enzymes have a broad substrate specificity. This suggests that the BR biosynthetic pathway consists of a metabolic grid rather than two separate parallel pathways.

1 This work was supported by the RIKEN Special Postdoctoral Researchers Program and by Grants-in-Aid for Scientific Research (no. 11640661 to Y.S. and no. 10460050 to S.F.) from the Ministry of Education, Science, Culture and Sports of Japan. Y.S. was a Special Postdoctoral Researcher at RIKEN. T.N. was supported by the Japan Society for the Promotion of Science. G.J.B. was supported as an STA (Royal Society) Research Fellow.

* Corresponding author; e-mail shimada{at}postman.riken.go.jp; fax 81-48-462-4959.

© 2001 American Society of Plant Physiologists


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