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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Main Authors: Martina Loi, Silvana De Leonardis, Giuseppina Mulè, Antonio F. Logrieco, Costantino Paciolla
Format: Article
Language:English
Published: MDPI AG 2020-05-01
Series:Antioxidants
Subjects:
Online Access:https://www.mdpi.com/2076-3921/9/5/435
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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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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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