title: A pathogenesis related-10 protein CaARP functions as aldo/keto reductase to scavenge cytotoxic aldehydes.
abstract: 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 yeast and fungi. We took three PR-10 proteins, CaARP from chickpea, ABR17 from pea and the major pollen allergen Bet v1 from silver birch as examples and showed that these purified recombinant proteins possessed AKR activity using various cytotoxic aldehydes including methylglyoxal and malondialdehyde as substrates and the reduced form of nicotinamide adenine dinucleotide phosphate (NADPH) as co-factor. Essential amino acids for this catalytic activity were identified by substitution with other amino acids. CaARP was able to discriminate between the reduced and oxidized forms of NADP independently of its catalytic activity and underwent structural change upon binding with NADPH. CaARP protein was preferentially localized in cytosol. When expressed in bacteria, yeast or plant, catalytically active variants of CaARP conferred tolerance to salinity, oxidative stress or cytotoxic aldehydes. CaARP-expressing plants showed lower lipid peroxidation product content in presence or absence of stress suggesting that the protein functions as a scavenger of cytotoxic aldehydes produced by metabolism and lipid peroxidation. Our result proposes a new biochemical property of a PR-10 protein.
authors.affiliation: National Institute of Plant Genome Research, Aruna Asaf Ali Marg, New Delhi, 110067, India.|Interdisciplinary Centre for Plant Genomics and Department of Plant Molecular Biology, University of Delhi South Campus, Benito Juarez Road, New Delhi, 110021, India.
authors.forename: Deepti
authors.initials: D
authors.lastname: Jain
authors.affiliation: National Institute of Plant Genome Research, Aruna Asaf Ali Marg, New Delhi, 110067, India.
authors.forename: Hitaishi
authors.initials: H
authors.lastname: Khandal
authors.affiliation: Interdisciplinary Centre for Plant Genomics and Department of Plant Molecular Biology, University of Delhi South Campus, Benito Juarez Road, New Delhi, 110021, India.
authors.forename: Jitendra Paul
authors.initials: JP
authors.lastname: Khurana
authors.affiliation: National Institute of Plant Genome Research, Aruna Asaf Ali Marg, New Delhi, 110067, India. debasis@nipgr.ac.in.
authors.forename: Debasis
authors.initials: D
authors.lastname: Chattopadhyay
mesh_terms: D000449:Aldehyde Reductase / Q000235:genetics / Q000378:metabolism*; D000447:Aldehydes / Q000378:metabolism; D000074408:Aldo-Keto Reductases; D000595:Amino Acid Sequence; D017360:Arabidopsis / Q000201:enzymology / Q000235:genetics / Q000502:physiology; D002384:Catalysis; D029863:Cicer / Q000201:enzymology* / Q000235:genetics / Q000502:physiology; D015227:Lipid Peroxidation; D008315:Malondialdehyde / Q000378:metabolism; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D010940:Plant Proteins / Q000235:genetics / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins; D055049:Salt Tolerance; D016415:Sequence Alignment
chemical_list: D000447:Aldehydes; D010940:Plant Proteins; D011994:Recombinant Proteins; C053376:pathogenesis-related proteins, plant; D008315:Malondialdehyde; D000074408:Aldo-Keto Reductases; D000449:Aldehyde Reductase
keywords: Aldo/keto reductase; Bet v1; CaARP; Cicer arietinum; PR-10