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Complementary DNA Cloning and Characterization of Ferredoxin Localized in Bundle-Sheath Cells of Maize Leaves1

Tomohiro Matsumura2, Yoko Kimata-Ariga*, Hitoshi Sakakibara, Tatsuo Sugiyama, Hiroshi Murata, Toshifumi Takao, Yasutsugu Shimonishi, and Toshiharu Hase

Division of Enzymology (T.M., Y.K.-A., T.H.), and Division of Organic Chemistry (H.M., T.T., Y.S.), Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871 Japan; and Institute for Protein Research, Osaka University, 3-2 Yamadaoka, Suita, Osaka, 565-0871 JapanDepartment of Biological Mechanisms and Functions, Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, 464-8601 Japan (H.S., T.S.)

In maize (Zea mays L.) two leaf-specific ferredoxin (Fd) isoproteins, Fd I and Fd II, are distributed differentially in mesophyll and bundle-sheath cells. A novel cDNA encoding the precursor of Fd II (pFD2) was isolated by heterologous hybridization using a cDNA for Fd I (pFD1) as a probe. The assignment of the cDNAs to the Fds was verified by capillary liquid-chromatography/electrospray ionization-mass spectrometry. RNA-blot analysis demonstrated that transcripts for Fd I and Fd II accumulated specifically in mesophyll and bundle-sheath cells, respectively. The mature regions of pFD1 and pFD2 were expressed in Escherichia coli as functional Fds. Fd I and Fd II had similar redox potentials of -423 and -406 mV, respectively, but the Km value of Fd-NADP+ reductase for Fd II was about 3-fold larger than that for Fd I. Asparagine at position 65 of Fd II is a unique residue compared with Fd I and other Fds from various plants, which have aspartic acid or glutamic acid at the corresponding position as an electrostatic interaction site with Fd-NADP+ reductase. Substitution of asparagine-65 with aspartic acid increased the affinity of Fd II with Fd-NADP+ reductase to a level comparable to that of Fd I. These structural and functional differences of Fd I and Fd II may be related to their cell-specific expression in the leaves of a C4 plant.

1   This work was supported in part by Grants-in-Aid for Research on Priority Areas (nos. 09274101 and 09274102 to T.S. and 09274101 and 09274103 to T.H.) from the Ministry of Education, Science and Culture of Japan.
2   Present address: Department of Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyo-ku, Tokyo, 113-8602 Japan.
*   Corresponding author; e-mail a-yoko{at}protein.osaka-u.ac.jp; fax 81-6-879-8613.

Plant Physiol. (1999) 119: 481-488
Copyright Clearance Center:   0032-0889/99/119//08
© 1999 American Society of Plant Physiologists




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