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Plant and Cell Physiology, 2002, Vol. 43, No. 7 706-717
© 2002 Oxford University Press

Identifying and Characterizing Plastidic 2-Oxoglutarate/Malate and Dicarboxylate Transporters in Arabidopsis thaliana

Mitsutaka Taniguchi1,5, Yojiro Taniguchi1, Michio Kawasaki1, Satomi Takeda2, Tomohiko Kato3, Shusei Sato3, Satoshi Tabata3, Hiroshi Miyake1 and Tatsuo Sugiyama4

1 Graduate School of Bioagricultural Sciences, Nagoya University, Nagoya, Aichi, 464-8601 Japan
2 Faculty of Science, Osaka Women’s University, Sakai, Osaka, 590-0035 Japan
3 Kazusa DNA Research Institute, Kisarazu, Chiba, 292-0812 Japan
4 RIKEN Plant Science Center, Yokohama, Kanagawa, 230-0045 Japan

We characterized three Arabidopsis genes, AtpOMT1, AtpDCT1 and AtpDCT2, localized on chromosome 5 and homologous to spinach chloroplastic 2-oxoglutarate/malate transporter (OMT) gene. The yeast-expressed recombinant AtpOMT1 protein transported malate and 2-oxoglutarate but not glutamate. By contrast, the recombinant AtpDCT1 protein transported 2-oxoglutarate and glutamate at similar affinities in exchange for malate. These findings suggested that AtpOMT1 is OMT and AtpDCT1 is a general dicarboxylate transporter (DCT). The recombinant proteins could also transport oxaloacetate at the same binding sites for dicarboxylates. In particular, the AtpOMT1 had a Km value for oxaloacetate one order of magnitude lower than those for malate and 2-oxoglutarate. Although the transcripts for the three genes were accumulated in all tissues examined, the expression of the genes in leaf tissues was light inducible. The expression of the three genes was also induced by nitrate supplement but the induction was most prominent and transient in AtpOMT1 similar to nitrate reductase gene. These findings lead to a proposition that AtpOMT1 functions as an oxaloacetate transporter in the malate–oxaloacetate shuttle across chloroplast membranes. We identified T-DNA insertional mutants of AtpOMT1 and AtpDCT1. Although the AtpOMT1 mutants could grow normally in normal air, the AtpDCT1 mutants were non-viable under the same conditions. The AtpDCT1 mutants were able to grow under the high CO2 condition to suppress photorespiration. These findings suggested that at least AtpDCT1 is a necessary component for photorespiratory nitrogen recycling.

5 Corresponding author: E-mail, taniguti@agr.nagoya-u.ac.jp; Fax, +81-52-789-4063.


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