Molecular cloning and characterization of a rice dehydroascorbate reductase

FEBS Letters

Tanaka, Kunisuke⁴  Nakagawa, Tomofumi¹  Ushimaru, Takashi¹  Urano, Jun'ichi¹  Masumura, Takehiro⁴  Maki, Yasushi³  Murata, Norio² 

[1] Department of Biology, Faculty of Science, Shizuoka University, Shizuoka 422-8529, Japan;National Institute for Basic Biology, Okazaki 444-8585, Japan;Department of Physics, Osaka Medical Collage, Osaka 569-0084, Japan;Laboratory of Genetic Engineering, Faculty of Agriculture, Kyoto Prefectural University, Kyoto 606-8522, Japan

关键词: Ascorbate;    Dehydroascorbate reductase;    Rice;    DHA;    dehydroascorbate;    DHAR;    dehydroascorbate reductase;    EST;    expression sequence tag;    GSH;    reduced glutathione;    PDI;    protein disulfide isomerase;    SDS-PAGE;    sodium dodecyl sulfate-polyacrylamide gel electrophoresis;   

DOI  :  10.1016/S0014-5793(99)01768-8

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Plant dehydroascorbate reductase (DHAR), which re-reduces oxidized ascorbate to maintain an appropriate level of ascorbate, is very important, but no gene or cDNA for plant DHAR has been cloned yet. Here, we describe a cDNA for a rice glutathione-dependent DHAR (designated DHAR1). A recombinant Dhar1p produced in Escherichia coli was functional. The expression sequence tag database suggests that Dhar1p homologs exist in various plants. Furthermore, the rice Dhar1p has a low similarity to rat DHAR, although the rice enzyme has a considerably higher specific activity than the mammalian one. The mRNA level of DHAR1, the protein level of Dhar1p and the DHAR activity in rice seedlings were elevated by high temperature, suggesting the protection role of DHAR at high temperature.

【 授权许可】

Unknown