A pathogenesis related-10 protein CaARP functions as aldo/keto reductase to scavenge @entity137 XXXX .

@entity3534 @entity14625 @entity137 @entity575 @entity1110 @entity1234 @entity3125 @entity375 @entity3587 @entity13474
UNASSIGNED: Pathogenesis related-10 (PR-10) proteins are present as multigene family in most of the higher plants. The role of PR-10 proteins in plant is poorly understood. A sequence analysis revealed that a large number of PR-10 proteins possess conserved motifs found in aldo/keto reductases (AKRs) of @entity375 and fungi. We took three PR-10 proteins, CaARP from @entity13474 , ABR17 from @entity3587 and the major pollen allergen Bet v1 from @entity575 birch as examples and showed that these purified recombinant proteins possessed AKR activity using various @entity137 @entity3125 including @entity14625 and @entity1234 as substrates and the reduced form of @entity1110 ( @entity1110 ) as co-factor. Essential @entity3534 for this catalytic activity were identified by substitution with other @entity3534 . CaARP was able to discriminate between the reduced and oxidized forms of @entity1110 independently of its catalytic activity and underwent structural change upon binding with @entity1110 . CaARP protein was preferentially localized in cytosol. When expressed in bacteria, @entity375 or plant, catalytically active variants of CaARP conferred tolerance to salinity, oxidative stress or @entity137 @entity3125 . CaARP-expressing plants showed lower lipid peroxidation product content in presence or absence of stress suggesting that the protein functions as a scavenger of @entity137 @entity3125 produced by metabolism and lipid peroxidation. Our result proposes a new biochemical property of a PR-10 protein.
