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4. The chaperone-like protein CDC48 regulates ascorbate peroxidase in tobacco

Author

Begue, Hervé, Besson-Bard, Angelique, Blanchard, Cécile, Winckler, Pascale, Bourque, Stéphane, Nicolas, Valérie, Wendehenne, David, ROSNOBLET, Claire, Agroécologie [Dijon], Université de Bourgogne (UB)-Institut National de la Recherche Agronomique (INRA)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Procédés Alimentaires et Microbiologiques [Dijon] (PAM), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, Dispositif Inter-régional d'Imagerie Cellulaire [Dijon] (DImaCell), Procédés Alimentaires et Microbiologiques (PAM), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Ingénierie et biologie cellulaire et tissulaire (IBCT (ex IFR133)), Centre Hospitalier Régional Universitaire de Besançon (CHRU Besançon)-Etablissement français du sang [Bourgogne-Franche-Comté] (EFS [Bourgogne-Franche-Comté])-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC)-Centre Hospitalier Régional Universitaire de Besançon (CHRU Besançon)-Etablissement français du sang [Bourgogne-Franche-Comté] (EFS [Bourgogne-Franche-Comté])-Université de Franche-Comté (UFC), Université Bourgogne Franche-Comté [COMUE] (UBFC)-Université Bourgogne Franche-Comté [COMUE] (UBFC), La Region Bourgogne (PARI AGREE), French Ministry of Higher Education, Research and Innovation, Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Université Bourgogne Franche-Comté [COMUE] (UBFC), Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement-Université Bourgogne Franche-Comté [COMUE] (UBFC), and Centre Hospitalier Régional Universitaire [Besançon] (CHRU Besançon)-Etablissement français du sang [Bourgogne-France-Comté] (EFS [Bourgogne-France-Comté])-Université de Franche-Comté (UFC)-Centre Hospitalier Régional Universitaire [Besançon] (CHRU Besançon)-Etablissement français du sang [Bourgogne-France-Comté] (EFS [Bourgogne-France-Comté])-Université de Franche-Comté (UFC)

Subjects
CDC48, Cell Biology, Research Papers, tobacco, cryptogein, protein-protein interaction, redox regulation, Ascorbate Peroxidases, Cytosol, protein–protein interaction, Gene Expression Regulation, Plant, Valosin Containing Protein, plant biochemistry, Ascorbate peroxidase, [SPI.GPROC]Engineering Sciences [physics]/Chemical and Process Engineering, [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology, MESH: Ascorbate peroxidase, Molecular Chaperones
Abstract

The ATPase NtCDC48 interacts with cytosolic ascorbate peroxidase, cAPX, and regulates its accumulation and activity in the immune response elicited by cryptogein in tobacco cells, and in the response to heat shock., There is increasing evidence that the chaperone-like protein CDC48 (cell division cycle 48) plays a role in plant immunity. Cytosolic ascorbate peroxidase (cAPX), which is a major regulator of the redox status of plant cells, has previously been shown to interact with CDC48. In this study, we examined the regulation of cAPX by the ATPase NtCDC48 during the cryptogein-induced immune response in tobacco cells. Our results not only confirmed the interaction between the proteins but also showed that it occurs in the cytosol. cAPX accumulation was modified in cells overexpressing NtCDC48, a process that was shown to involve post-translational modification of cAPX. In addition, cryptogein-induced increases in cAPX activity were suppressed in cells overexpressing NtCDC48 and the abundance of the cAPX dimer was below the level of detection. Furthermore, the levels of both reduced (GSH) and oxidized glutathione (GSSG) and the GSH/GSSG ratio decreased more rapidly in response to the elicitor in these cells than in controls. A decrease in cAPX activity was also observed in response to heat shock in the cells overexpressing NtCDC48, indicating that the regulation of cAPX by NtCDC48 is not specific to the immune response.

Published
2019

6. Opinions

Author

Blanchard, Cécile, primary, Eydoux, Anne, additional, Turner, Adair, additional, and Aggeri, Franck, additional

Published
2019
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7. Opinions

Author

Gadrey, Jean, primary, Eydoux, Anne, additional, Blanchard, Cécile, additional, and Aggeri, Franck, additional

Published
2019
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8. Study of the chaperone protein CDC48 involvement in plant immunity

Author

Begue, Hervé, Blanchard, Cécile, Rosnoblet, Claire, Wendehenne, David, Agroécologie [Dijon], Institut National de la Recherche Agronomique (INRA)-Université de Bourgogne (UB)-AgroSup Dijon - Institut National Supérieur des Sciences Agronomiques, de l'Alimentation et de l'Environnement, and Institut National de la Recherche Agronomique (INRA). FRA.

Subjects
CDC48, [SDV]Life Sciences [q-bio], [SDE]Environmental Sciences, [SDV.BV]Life Sciences [q-bio]/Vegetal Biology, interaction protein-protein, plant immunity, cAPX, cryptogein
Abstract

CDC48 is a conserved chaperone protein belonging to the AAA+ ATPase family (ATPase associated with various activities). This protein uses binding and hydrolysis of ATP to generate forces to affect the transformation of polypeptide substrate in numerous cellular processes. Studies on mammalian CDC48 orthologue revealed that it recognizes ubiquitylated polypeptides, directly or via partners, leading to substrate degradation or recycling. In plants, functions of CDC48 is less understood. The aim of my thesis, is to decipher the role of CDC48 in plant defense response context. First, I have to characterize NtCDC48 in tobacco (Nicotiana tabacum) suspension cells elicited by cryptogein, an elicitin produced by the oomycete Phytophthora cryptogea. Secondly, I have to confirm interactions with different partners previously established by the team, after that, I have to study involvement of those partners in plant immunity. As expected, those partners contribute in diverse cellular processes. Currently, I focus my attention on the interaction between NtCDC48 and the cytosolic ascorbate peroxidase (cAPX), a protein involved on the detoxification of reactive oxygen species. Our first results indicate that CDC48 protein and mRNA accumulate during cryptogein treatment, highlighting that the chaperone protein is involved in immune response. Then, thanks to a cell line overexpressing our protein of interest, we propose that NtCDC48 might have a function in the elicitor-triggered cell death.

Published
2016

9. chaperone-like protein CDC48 regulates ascorbate peroxidase in tobacco.

Author

Bègue, Hervé, Besson-Bard, Angélique, Blanchard, Cécile, Winckler, Pascale, Bourque, Stéphane, Nicolas, Valérie, Wendehenne, David, and Rosnoblet, Claire

Subjects
PEROXIDASE, POST-translational modification, DISEASE resistance of plants, CELL division, TOBACCO, MECHANICAL shock measurement
Abstract

There is increasing evidence that the chaperone-like protein CDC48 (cell division cycle 48) plays a role in plant immunity. Cytosolic ascorbate peroxidase (cAPX), which is a major regulator of the redox status of plant cells, has previously been shown to interact with CDC48. In this study, we examined the regulation of cAPX by the ATPase NtCDC48 during the cryptogein-induced immune response in tobacco cells. Our results not only confirmed the interaction between the proteins but also showed that it occurs in the cytosol. cAPX accumulation was modified in cells overexpressing NtCDC48, a process that was shown to involve post-translational modification of cAPX. In addition, cryptogein-induced increases in cAPX activity were suppressed in cells overexpressing NtCDC48 and the abundance of the cAPX dimer was below the level of detection. Furthermore, the levels of both reduced (GSH) and oxidized glutathione (GSSG) and the GSH/GSSG ratio decreased more rapidly in response to the elicitor in these cells than in controls. A decrease in cAPX activity was also observed in response to heat shock in the cells overexpressing NtCDC48, indicating that the regulation of cAPX by NtCDC48 is not specific to the immune response. [ABSTRACT FROM AUTHOR]

Published
2019
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10. The chaperone-like protein CDC48 regulates ascorbate peroxidase in tobacco.

Author

Bègue H, Besson-Bard A, Blanchard C, Winckler P, Bourque S, Nicolas V, Wendehenne D, and Rosnoblet C

Subjects
Ascorbate Peroxidases metabolism, Cytosol metabolism, Molecular Chaperones metabolism, Nicotiana enzymology, Valosin Containing Protein metabolism, Ascorbate Peroxidases genetics, Gene Expression Regulation, Plant, Nicotiana genetics, Valosin Containing Protein genetics
Abstract

There is increasing evidence that the chaperone-like protein CDC48 (cell division cycle 48) plays a role in plant immunity. Cytosolic ascorbate peroxidase (cAPX), which is a major regulator of the redox status of plant cells, has previously been shown to interact with CDC48. In this study, we examined the regulation of cAPX by the ATPase NtCDC48 during the cryptogein-induced immune response in tobacco cells. Our results not only confirmed the interaction between the proteins but also showed that it occurs in the cytosol. cAPX accumulation was modified in cells overexpressing NtCDC48, a process that was shown to involve post-translational modification of cAPX. In addition, cryptogein-induced increases in cAPX activity were suppressed in cells overexpressing NtCDC48 and the abundance of the cAPX dimer was below the level of detection. Furthermore, the levels of both reduced (GSH) and oxidized glutathione (GSSG) and the GSH/GSSG ratio decreased more rapidly in response to the elicitor in these cells than in controls. A decrease in cAPX activity was also observed in response to heat shock in the cells overexpressing NtCDC48, indicating that the regulation of cAPX by NtCDC48 is not specific to the immune response., (© The Author(s) 2019. Published by Oxford University Press on behalf of the Society for Experimental Biology.)

Published
2019
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