A pathogenesis related-10 protein CaARP functions as aldo/keto reductase to scavenge cytotoxic aldehydes
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Title |
A pathogenesis related-10 protein CaARP functions as aldo/keto reductase to scavenge cytotoxic aldehydes
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Creator |
Jain, Deepti
Khandal, Hitaishi Khurana, Jitendra Paul Chattopadhyay, Debasis |
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Subject |
PR-10
CaARP Bet v1 Aldo/keto reductase Cicer arietinum |
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Description |
Accepted date: 6 November 2015
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 acknowledge Dr. Alok K. Sinha and Dr. Arsheed H. Seikh, NIPGR for Bet v1 clone. No conflict of interest declared. DJ acknowledges INSPIRE faculty program of Department of Science and Technology (DST), Government of India. HK acknowledges Council of Scientific and Industrial Research, India for fellowship. This work was supported by the core grant from National Institute of Plant Genome Research (NIPGR), New Delhi, India. |
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Date |
2015-12-31T09:40:02Z
2015-12-31T09:40:02Z 2016 |
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Type |
Article
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Identifier |
Plant Mol. Biol., 90(1-2): 171-187
1573-5028 http://172.16.0.77:8080/jspui/handle/123456789/482 http://link.springer.com/article/10.1007%2Fs11103-015-0405-z 10.1007/s11103-015-0405-z |
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Language |
en_US
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Publisher |
Springer
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