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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Gene Review: 

ATR2  -  NADPH--cytochrome P450 reductase 2

Arabidopsis thaliana

Synonyms: AR2, F9N11.60, F9N11_60, P450 reductase 2
 
 
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Disease relevance of ATR2

  • An N-terminally modified form of the Arabidopsis NADPH-cytochrome P450 ATR2 (ATR2mod) was expressed from the tactac promoter in Escherichia coli to obtain high yields of the enzyme [1].
  • Moreover, overexpression of mutant atr2D, but not wild-type ATR2, conferred pleiotropic effects, including reduced size, dark pigmentation, and sterility [2].
 

High impact information on ATR2

  • ATR1 encodes a protein of 692 amino acids, while ATR2 encodes either a 712-residue protein (ATR2-1), or a 702-residue protein (ATR2-2) depending on the choice of the initiation codon [3].
  • Analysis of reductase kinetic properties using artificial acceptors and different salt conditions suggested marked differences between reductases in their FAD and FMN environments and confirmed the unusual properties of the ATR2 FMN-binding domain [4].
  • Following the fast phase of reduction, expected accumulation of flavin semiquinone was observed for the human and ATR1 but not for ATR2 and the yeast reductases [4].

References

  1. Bacterial expression and purification of the Arabidopsis NADPH-cytochrome P450 reductase ATR2. Hull, A.K., Celenza, J.L. Protein Expr. Purif. (2000) [Pubmed]
  2. Dominant alleles of the basic helix-loop-helix transcription factor ATR2 activate stress-responsive genes in Arabidopsis. Smolen, G.A., Pawlowski, L., Wilensky, S.E., Bender, J. Genetics (2002) [Pubmed]
  3. Cloning, yeast expression, and characterization of the coupling of two distantly related Arabidopsis thaliana NADPH-cytochrome P450 reductases with P450 CYP73A5. Urban, P., Mignotte, C., Kazmaier, M., Delorme, F., Pompon, D. J. Biol. Chem. (1997) [Pubmed]
  4. Differential redox and electron-transfer properties of purified yeast, plant and human NADPH-cytochrome P-450 reductases highly modulate cytochrome P-450 activities. Louërat-Oriou, B., Perret, A., Pompon, D. Eur. J. Biochem. (1998) [Pubmed]
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