Molecular cloning and characterization of a rice dehydroascorbate reductase

FEBS Lett. 2000 Jan 21;466(1):107-11. doi: 10.1016/s0014-5793(99)01768-8.

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.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Base Sequence
  • Cloning, Molecular
  • DNA, Complementary / genetics
  • DNA, Plant / genetics
  • Escherichia coli / genetics
  • Genes, Plant
  • Hot Temperature
  • Humans
  • Molecular Sequence Data
  • Oryza / enzymology*
  • Oryza / genetics*
  • Oxidoreductases / genetics*
  • Oxidoreductases / metabolism
  • RNA, Messenger / genetics
  • RNA, Messenger / metabolism
  • RNA, Plant / genetics
  • RNA, Plant / metabolism
  • Rats
  • Recombinant Proteins / genetics
  • Recombinant Proteins / metabolism
  • Sequence Homology, Amino Acid

Substances

  • DNA, Complementary
  • DNA, Plant
  • RNA, Messenger
  • RNA, Plant
  • Recombinant Proteins
  • Oxidoreductases
  • glutathione dehydrogenase (ascorbate)