Plant Physiology 132:1989-1997 (2003)
© 2003 American Society of Plant Biologists
ENVIRONMENTAL STRESS AND ADAPTATION
Three Nicotianamine Synthase Genes Isolated from Maize Are Differentially Regulated by Iron Nutritional Status
Daichi Mizuno,
Kyoko Higuchi,
Tatsuya Sakamoto,
Hiromi Nakanishi,
Satoshi Mori and
Naoko K. Nishizawa*
Departments of Applied Biological Chemistry (D.M., K.H., H.N., S.M.) and
Global Agricultural Sciences (T.S., N.K.N.), Graduate School of Agricultural
and Life Science, University of Tokyo, 1–1–1 Yayoi, Bunkyoku,
Tokyo 113–8657, Japan; and Core Research for Evolutional Science and
Technology, Japan Science and Technology Corporation, 2–1–6
Sengen, Tsukuba 305–0047, Japan (K.H., S.M., N.K.N.)
Nicotianamine synthase (NAS) is an enzyme that is critical for the
biosynthesis of the mugineic acid family of phytosiderophores in graminaceous
plants, and for the homeostasis of metal ions in nongraminaceous plants. We
isolated one genomic NAS clone, ZmNAS3, and two cDNA
NAS clones, ZmNAS1 and ZmNAS2, from maize (Zea
mays cv Alice). In agreement with the increased secretion of
phytosiderophores with Fe deficiency, ZmNAS1 and ZmNAS2 were
positively expressed only in Fe-deficient roots. In contrast, ZmNAS3
was expressed under Fe-sufficient conditions, and was negatively regulated by
Fe deficiency. This is the first report describing down-regulation of
NAS gene expression in response to Fe deficiency in plants, shedding
light on the role of nicotianamine in graminaceous plants, other than as a
precursor in phytosiderophore production. ZmNAS1-green fluorescent protein
(sGFP) and ZmNAS2-sGFP were localized at spots in the cytoplasm of onion
(Allium cepa) epidermal cells, whereas ZmNAS3-sGFP was distributed
throughout the cytoplasm of these cells. ZmNAS1 and ZmNAS3 showed NAS activity
in vitro, whereas ZmNAS2 showed none. Due to its duplicated structure, ZmNAS2
was much larger (65.8 kD) than ZmNAS1, ZmNAS3, and previously characterized
NAS proteins (30–38 kD) from other plant species. We reveal that maize
has two types of NAS proteins based on their expression pattern and
subcellular localization.
Article, publication date, and citation information can be found at
www.plantphysiol.org/cgi/doi/10.1104/pp.102.019869.
*
Corresponding author; e-mail
annaoko{at}mail.ecc.u-tokyo.ac.jp;
fax 813–5841–5337.
Received December 29, 2002;
returned for revision February 25, 2003;
accepted May 12, 2003.
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