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Cloning of Nicotianamine Synthase Genes, Novel Genes Involved in the Biosynthesis of Phytosiderophores

Kyoko Higuchi, Kazuya Suzuki, Hiromi Nakanishi, Hirotaka Yamaguchi, Naoko-Kishi Nishizawa, and Satoshi Mori*

Laboratory of Plant Molecular Physiology, Department of Applied Biological Chemistry, The University of Tokyo, 1-1 Yayoi, Bunkyo-ku, 113-8657 Tokyo, Japan (K.H., K.S., H.N., H.Y., N.-K.N., S.M.); and Core Research for Evolutional Science and Technology, Japan Science and Technology Corporation, 4-1-8 Honcho, Kawaguchi-shi, 332-0012, Saitama, Japan (K.H., K.S., H.Y., S.M.)

Nicotianamine synthase (NAS), the key enzyme in the biosynthetic pathway for the mugineic acid family of phytosiderophores, catalyzes the trimerization of S-adenosylmethionine to form one molecule of nicotianamine. We purified NAS protein and isolated the genes nas1, nas2, nas3, nas4, nas5-1, nas5-2, and nas6, which encode NAS and NAS-like proteins from Fe-deficient barley (Hordeum vulgare L. cv Ehimehadaka no. 1) roots. Escherichia coli expressing nas1 showed NAS activity, confirming that this gene encodes a functional NAS. Expression of nas genes as determined by northern-blot analysis was induced by Fe deficiency and was root specific. The NAS genes form a multigene family in the barley and rice genomes.

*   Corresponding author; e-mail asmori{at}hongo.ecc.u-tokyo.ac.jp; fax 81-3-3812-0544.

Plant Physiol. (1999) 119: 471-480
Copyright Clearance Center:   0032-0889/99/119//10
© 1999 American Society of Plant Physiologists




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