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Gene Review:

MDHAR - monodehydroascorbate reductase (NADH)

Arabidopsis thaliana

Synonyms: ARABIDOPSIS THALIANA MONODEHYDROASCORBATE REDUCTASE 3, ATMDAR3, F8A24.20, MDAR2, MDAR3, ...

Lisenbee, C.S. et al., Obara, K. et al., Baier, M. et al.

Obara, Sumi, Fukuda, Baier, Noctor, Foyer, Dietz,

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High impact information on MDHAR

The PTS1-dependent sorting of AtMDAR1 and PsMDAR to peroxisomes was incomplete (inefficient?), but was improved for PsMDAR after changing its PTS1 sequence from -SKI to the canonical tripeptide -SKL [1].
The H2O2 byproduct of fatty acid catabolism in plant peroxisomes is removed in part by a membrane-associated antioxidant system that involves both an ascorbate peroxidase and a monodehydroascorbate reductase (MDAR) [1].
Despite descriptions of 32-kDa MDAR polypeptides in pea and castor peroxisomal membranes and cDNA sequences for several 'cytosolic' MDARs, the genetic and protein factors responsible for peroxisomal MDAR function have yet to be elucidated [1].
The use of multiple transcription starts causes the dual targeting of Arabidopsis putative monodehydroascorbate reductase to both mitochondria and chloroplasts [2].
Monodehydroascorbate reductase (MDAR) isoforms exist in mitochondria, chloroplasts, cytosol and microbodies [2].

Anatomical context of MDHAR

The activities of thylakoid and stromal ascorbate peroxidase and particularly monodehydroascorbate reductase were increased as were transcripts for these enzymes [3].
These results demonstrate that putative MDAR is a dual-targeting protein transported into both mitochondria and chloroplasts [2].

References

Arabidopsis peroxisomes possess functionally redundant membrane and matrix isoforms of monodehydroascorbate reductase. Lisenbee, C.S., Lingard, M.J., Trelease, R.N. Plant J. (2005) [Pubmed]
The use of multiple transcription starts causes the dual targeting of Arabidopsis putative monodehydroascorbate reductase to both mitochondria and chloroplasts. Obara, K., Sumi, K., Fukuda, H. Plant Cell Physiol. (2002) [Pubmed]
Antisense suppression of 2-cysteine peroxiredoxin in Arabidopsis specifically enhances the activities and expression of enzymes associated with ascorbate metabolism but not glutathione metabolism. Baier, M., Noctor, G., Foyer, C.H., Dietz, K.J. Plant Physiol. (2000) [Pubmed]

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