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Molecular and biochemical characterization of dehydroascorbate reductase from a stress adapted C4 plant, pearl millet [Pennisetum glaucum (L.) R. Br].

Authors
  • Pandey, Prachi
  • Achary, V Mohan Murali
  • Kalasamudramu, Vani
  • Mahanty, Srikrishna
  • Reddy, Guda Maheedhara
  • Reddy, Malireddy K
Type
Published Article
Journal
Plant Cell Reports
Publisher
Springer-Verlag
Publication Date
Mar 01, 2014
Volume
33
Issue
3
Pages
435–445
Identifiers
DOI: 10.1007/s00299-013-1544-9
PMID: 24317405
Source
Medline
License
Unknown

Abstract

Dehydroascorbate reductase (EC 1.8.5.1) is a crucial enzyme actively involved in the recycling of ascorbate redox pool in the cellular environment. In this study, the full-length cDNA coding for DHAR polypeptide and its corresponding gene was isolated from Pennisetum glaucum (PgDHAR). PgDHAR encodes a polypeptide of 213 amino acids with a predicted molecular mass of 23.4 kDa and shares 80-75 % sequence homology with DHAR from other plants. The heterologously expressed recombinant PgDHAR protein exhibited activity in a wide range of substrate concentrations. The recombinant PgDHAR is thermostable and retains its activity over a broad pH range. Furthermore, transcript level of PgDHAR is quantitatively up-regulated in response to temperature. On the whole, PgDHAR alone or in combination with other genes of ascorbate-glutathione cycle can be used for the development of stress tolerant as well as nutritionally improved food crop with enhanced ascorbic acid content.

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