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| Title: Molecular cloning and characterization of a rice dehydroascorbate reductase .
| | Author: Urano J Nakagawa T Maki Y Masumura T Tanaka K Murata N Ushimaru T | | Journal: FEBS Lett .
Citation: V : 466 ( 1 ) P : 107-11 Year: 2000 Type: ARTICLE | | Literature: oryza Field: abstract Doc ID: pub10648822 Accession (PMID): 10648822 | | Abstract: 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 . | Matching Sentences:
[ Sen. 3, subscore: 2.00 ]: A recombinant Dhar1p produced in Escherichia coli was functional The expression sequence tag database suggests that Dhar1p homologs exist in various plants .
[ Sen. 5, subscore: 2.00 ]: 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 .
[ Sen. 2, subscore: 1.00 ]: Here , we describe a cDNA for a rice glutathione-dependent DHAR ( designated DHAR1 ) .
[ Sen. 4, subscore: 1.00 ]: 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 .
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