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Molecular cloning and characterization of a rice dehydroascorbate reductase
Author(s) -
Urano Jun'ichi,
Nakagawa Tomofumi,
Maki Yasushi,
Masumura Takehiro,
Tanaka Kunisuke,
Murata Norio,
Ushimaru Takashi
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01768-8
Subject(s) - complementary dna , escherichia coli , biochemistry , molecular cloning , cloning (programming) , biology , gene , glutathione , enzyme , recombinant dna , microbiology and biotechnology , chemistry , computer science , programming language
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.