A Novel and Potentially Multifaceted Dehydroascorbate Reductase Increasing the Antioxidant Systems is Induced by Beauvericin in Tomato
Dehydroascorbate reductases (DHARs) are important enzymes that reconvert the dehydroascorbic acid (DHA) into ascorbic acid (ASC). They are involved in the plant response to oxidative stress, such as that induced by the mycotoxin beauvericin (BEA). Tomato plants were treated with 50 µM of BEA; the ma...
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MDPI AG
2020-05-01
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author | Martina Loi Silvana De Leonardis Giuseppina Mulè Antonio F. Logrieco Costantino Paciolla |
author_facet | Martina Loi Silvana De Leonardis Giuseppina Mulè Antonio F. Logrieco Costantino Paciolla |
author_sort | Martina Loi |
collection | DOAJ |
description | Dehydroascorbate reductases (DHARs) are important enzymes that reconvert the dehydroascorbic acid (DHA) into ascorbic acid (ASC). They are involved in the plant response to oxidative stress, such as that induced by the mycotoxin beauvericin (BEA). Tomato plants were treated with 50 µM of BEA; the main antioxidant compounds and enzymes were evaluated. DHARs were analyzed in the presence of different electron donors by native and denaturing electrophoresis as well as by western blot and mass spectrometry to identify a novel induced protein with DHAR activity. Kinetic parameters for dehydroascorbate (DHA) and glutathione (GSH) were also determined. The novel DHAR was induced after BEA treatment. It was GSH-dependent and possessed lower affinity to DHA and GSH than the classical DHARs. Interestingly, the mass spectrometry analysis of the main band appearing on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) revealed a chloroplast sedoheptulose 1,7-bisphosphatase, a key enzyme of the Calvin cycle, and a chloroplast mRNA-binding protein, suggesting that the DHA reducing capacity could be a side activity or the novel DHAR could be part of a protein complex. These results shed new light on the ascorbate-glutathione regulation network under oxidative stress and may represent a new way to increase the plant antioxidant defense system, plant nutraceutical value, and the health benefits of plant consumption. |
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language | English |
last_indexed | 2024-03-10T19:47:44Z |
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spelling | doaj.art-886e0883d36d4d908b6fd65ecc2d6b782023-11-20T00:40:59ZengMDPI AGAntioxidants2076-39212020-05-019543510.3390/antiox9050435A Novel and Potentially Multifaceted Dehydroascorbate Reductase Increasing the Antioxidant Systems is Induced by Beauvericin in TomatoMartina Loi0Silvana De Leonardis1Giuseppina Mulè2Antonio F. Logrieco3Costantino Paciolla4Institute of Sciences of Food Production, National Research Council, Via G. Amendola 122/0, 70126 Bari, ItalyDepartment of Biology, University of Bari “Aldo Moro”, Via E. Orabona 4, 70125 Bari, ItalyInstitute of Sciences of Food Production, National Research Council, Via G. Amendola 122/0, 70126 Bari, ItalyInstitute of Sciences of Food Production, National Research Council, Via G. Amendola 122/0, 70126 Bari, ItalyDepartment of Biology, University of Bari “Aldo Moro”, Via E. Orabona 4, 70125 Bari, ItalyDehydroascorbate reductases (DHARs) are important enzymes that reconvert the dehydroascorbic acid (DHA) into ascorbic acid (ASC). They are involved in the plant response to oxidative stress, such as that induced by the mycotoxin beauvericin (BEA). Tomato plants were treated with 50 µM of BEA; the main antioxidant compounds and enzymes were evaluated. DHARs were analyzed in the presence of different electron donors by native and denaturing electrophoresis as well as by western blot and mass spectrometry to identify a novel induced protein with DHAR activity. Kinetic parameters for dehydroascorbate (DHA) and glutathione (GSH) were also determined. The novel DHAR was induced after BEA treatment. It was GSH-dependent and possessed lower affinity to DHA and GSH than the classical DHARs. Interestingly, the mass spectrometry analysis of the main band appearing on sodium dodecyl sulphate polyacrylamide gel electrophoresis (SDS-PAGE) revealed a chloroplast sedoheptulose 1,7-bisphosphatase, a key enzyme of the Calvin cycle, and a chloroplast mRNA-binding protein, suggesting that the DHA reducing capacity could be a side activity or the novel DHAR could be part of a protein complex. These results shed new light on the ascorbate-glutathione regulation network under oxidative stress and may represent a new way to increase the plant antioxidant defense system, plant nutraceutical value, and the health benefits of plant consumption.https://www.mdpi.com/2076-3921/9/5/435beauvericindehydroascorbate reductasetomato1,7-sedoheptulose bisphosphataseRNA-binding proteinantioxidants |
spellingShingle | Martina Loi Silvana De Leonardis Giuseppina Mulè Antonio F. Logrieco Costantino Paciolla A Novel and Potentially Multifaceted Dehydroascorbate Reductase Increasing the Antioxidant Systems is Induced by Beauvericin in Tomato Antioxidants beauvericin dehydroascorbate reductase tomato 1,7-sedoheptulose bisphosphatase RNA-binding protein antioxidants |
title | A Novel and Potentially Multifaceted Dehydroascorbate Reductase Increasing the Antioxidant Systems is Induced by Beauvericin in Tomato |
title_full | A Novel and Potentially Multifaceted Dehydroascorbate Reductase Increasing the Antioxidant Systems is Induced by Beauvericin in Tomato |
title_fullStr | A Novel and Potentially Multifaceted Dehydroascorbate Reductase Increasing the Antioxidant Systems is Induced by Beauvericin in Tomato |
title_full_unstemmed | A Novel and Potentially Multifaceted Dehydroascorbate Reductase Increasing the Antioxidant Systems is Induced by Beauvericin in Tomato |
title_short | A Novel and Potentially Multifaceted Dehydroascorbate Reductase Increasing the Antioxidant Systems is Induced by Beauvericin in Tomato |
title_sort | novel and potentially multifaceted dehydroascorbate reductase increasing the antioxidant systems is induced by beauvericin in tomato |
topic | beauvericin dehydroascorbate reductase tomato 1,7-sedoheptulose bisphosphatase RNA-binding protein antioxidants |
url | https://www.mdpi.com/2076-3921/9/5/435 |
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