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Formate Dehydrogenase, an Enzyme of Anaerobic Metabolism, Is
Induced by Iron Deficiency in Barley Roots1
Kazuya Suzuki,
Reiko Itai,
Koichiro Suzuki,
Hiromi Nakanishi,
Naoko-Kishi Nishizawa,
Etsuro Yoshimura, and
Satoshi Mori*
Laboratory of Plant Molecular Physiology, Department of Applied
Biological Chemistry, The University of Tokyo, 1-1 Yayoi, Bunkyo-ku,
113 Tokyo, Japan (R.I., H.N., N.-K.N., E.Y., S.M.); and Core Research
for Evolutional Science and Technology, Japan Science and Technology
Corporation, 2-1-6 Sengen, 305 Tsukuba, Japan (Ka.S., Ko.S.,
S.M.)
To identify the proteins induced by
Fe deficiency, we have compared the proteins of Fe-sufficient and
Fe-deficient barley (Hordeum vulgare L.) roots by
two-dimensional polyacrylamide gel electrophoresis. Peptide sequence
analysis of induced proteins revealed that formate dehydrogenase (FDH),
adenine phosphoribosyltransferase, and the Ids3
gene product (for Fe deficiency-specific) increased in Fe-deficient
roots. FDH enzyme activity was detected in Fe-deficient roots but not
in Fe-sufficient roots. A cDNA encoding FDH (Fdh) was
cloned and sequenced. Fdh expression was induced by Fe
deficiency. Fdh was also expressed under anaerobic
stress and its expression was more rapid than that induced by Fe
deficiency. Thus, the expression of Fdh observed in
Fe-deficient barley roots appeared to be a secondary effect caused by
oxygen deficiency in Fe-deficient plants.
1
This work has been supported by Core Research
for Evolutional Science and Technology, Japan Science and Technology
Corporation (Tsukuba, Japan).
*
Corresponding author; e-mail asmori{at}hongo.ecc.u-tokyo.ac.jp;
fax 81-3-5684-4822.
Plant Physiol. (1998) 116: 725-732
Copyright Clearance Center: 0032-0889/98/116/0725/08
© 1998 American Society of Plant Physiologists
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