Molecular cloning and characterization of a rice dehydroascorbate reductase

被引:93
|
作者
Urano, J
Nakagawa, T
Maki, Y
Masumura, T
Tanaka, K
Murata, N
Ushimaru, T [1 ]
机构
[1] Shizuoka Univ, Fac Sci, Dept Biol, Shizuoka 4228529, Japan
[2] Osaka Med Coll, Dept Phys, Osaka 5690084, Japan
[3] Kyoto Prefectural Univ, Fac Agr, Lab Genet Engn, Kyoto 6068522, Japan
[4] Kyoto Prefectural Inst Agr Biotechnol, Kyoto 6190244, Japan
[5] Natl Inst Basic Biol, Okazaki, Aichi 4448585, Japan
来源
FEBS LETTERS | 2000年 / 466卷 / 01期
关键词
ascorbate; dehydroascorbate reductase; rice;
D O I
10.1016/S0014-5793(99)01768-8
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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, (C) 2000 Federation of European Biochemical Societies.
引用
收藏
页码:107 / 111
页数:5
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