Complex Formation between the Transcription Factor WRKY53 and Antioxidative Enzymes Leads to Reciprocal Inhibition
The transcription factor WRKY53 of the model plant <i>Arabidopsis thaliana</i> is an important regulator of leaf senescence. Its expression, activity and degradation are tightly controlled by various mechanisms and feedback loops. Hydrogen peroxide is one of the inducing agents for <i...
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MDPI AG
2024-03-01
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author | Ana Gabriela Andrade Galan Jasmin Doll Natalie Faiß Patricia Weber Ulrike Zentgraf |
author_facet | Ana Gabriela Andrade Galan Jasmin Doll Natalie Faiß Patricia Weber Ulrike Zentgraf |
author_sort | Ana Gabriela Andrade Galan |
collection | DOAJ |
description | The transcription factor WRKY53 of the model plant <i>Arabidopsis thaliana</i> is an important regulator of leaf senescence. Its expression, activity and degradation are tightly controlled by various mechanisms and feedback loops. Hydrogen peroxide is one of the inducing agents for <i>WRKY53</i> expression, and a long-lasting intracellular increase in H<sub>2</sub>O<sub>2</sub> content accompanies the upregulation of <i>WRKY53</i> at the onset of leaf senescence. We have identified different antioxidative enzymes, including catalases (CATs), superoxide dismutases (SODs) and ascorbate peroxidases (APXs), as protein interaction partners of WRKY53 in a WRKY53-pulldown experiment at different developmental stages. The interaction of WRKY53 with these enzymes was confirmed in vivo by bimolecular fluorescence complementation assays (BiFC) in <i>Arabidopsis</i> protoplasts and transiently transformed tobacco leaves. The interaction with WRKY53 inhibited the activity of the enzyme isoforms CAT2, CAT3, APX1, Cu/ZuSOD1 and FeSOD1 (and vice versa)<i>,</i> while the function of WRKY53 as a transcription factor was also inhibited by these complex formations. Other WRKY factors like WRKY18 or WRKY25 had no or only mild inhibitory effects on the enzyme activities, indicating that WRKY53 has a central position in this crosstalk. Taken together, we identified a new additional and unexpected feedback regulation between H<sub>2</sub>O<sub>2,</sub> the antioxidative enzymes and the transcription factor WRKY53. |
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spelling | doaj.art-305503f6bea64fd9a67a579d0fd87c2a2024-03-27T13:18:33ZengMDPI AGAntioxidants2076-39212024-03-0113331510.3390/antiox13030315Complex Formation between the Transcription Factor WRKY53 and Antioxidative Enzymes Leads to Reciprocal InhibitionAna Gabriela Andrade Galan0Jasmin Doll1Natalie Faiß2Patricia Weber3Ulrike Zentgraf4Center for Plant Molecular Biology (ZMBP), University of Tuebingen, Auf der Morgenstelle 32, 72076 Tübingen, GermanyCenter for Plant Molecular Biology (ZMBP), University of Tuebingen, Auf der Morgenstelle 32, 72076 Tübingen, GermanyCenter for Plant Molecular Biology (ZMBP), University of Tuebingen, Auf der Morgenstelle 32, 72076 Tübingen, GermanyCenter for Plant Molecular Biology (ZMBP), University of Tuebingen, Auf der Morgenstelle 32, 72076 Tübingen, GermanyCenter for Plant Molecular Biology (ZMBP), University of Tuebingen, Auf der Morgenstelle 32, 72076 Tübingen, GermanyThe transcription factor WRKY53 of the model plant <i>Arabidopsis thaliana</i> is an important regulator of leaf senescence. Its expression, activity and degradation are tightly controlled by various mechanisms and feedback loops. Hydrogen peroxide is one of the inducing agents for <i>WRKY53</i> expression, and a long-lasting intracellular increase in H<sub>2</sub>O<sub>2</sub> content accompanies the upregulation of <i>WRKY53</i> at the onset of leaf senescence. We have identified different antioxidative enzymes, including catalases (CATs), superoxide dismutases (SODs) and ascorbate peroxidases (APXs), as protein interaction partners of WRKY53 in a WRKY53-pulldown experiment at different developmental stages. The interaction of WRKY53 with these enzymes was confirmed in vivo by bimolecular fluorescence complementation assays (BiFC) in <i>Arabidopsis</i> protoplasts and transiently transformed tobacco leaves. The interaction with WRKY53 inhibited the activity of the enzyme isoforms CAT2, CAT3, APX1, Cu/ZuSOD1 and FeSOD1 (and vice versa)<i>,</i> while the function of WRKY53 as a transcription factor was also inhibited by these complex formations. Other WRKY factors like WRKY18 or WRKY25 had no or only mild inhibitory effects on the enzyme activities, indicating that WRKY53 has a central position in this crosstalk. Taken together, we identified a new additional and unexpected feedback regulation between H<sub>2</sub>O<sub>2,</sub> the antioxidative enzymes and the transcription factor WRKY53.https://www.mdpi.com/2076-3921/13/3/315catalase (CAT)ascorbate peroxidase (APX)superoxide dismutase (SOD)WRKY transcription factorsWRKY53protein–protein interaction |
spellingShingle | Ana Gabriela Andrade Galan Jasmin Doll Natalie Faiß Patricia Weber Ulrike Zentgraf Complex Formation between the Transcription Factor WRKY53 and Antioxidative Enzymes Leads to Reciprocal Inhibition Antioxidants catalase (CAT) ascorbate peroxidase (APX) superoxide dismutase (SOD) WRKY transcription factors WRKY53 protein–protein interaction |
title | Complex Formation between the Transcription Factor WRKY53 and Antioxidative Enzymes Leads to Reciprocal Inhibition |
title_full | Complex Formation between the Transcription Factor WRKY53 and Antioxidative Enzymes Leads to Reciprocal Inhibition |
title_fullStr | Complex Formation between the Transcription Factor WRKY53 and Antioxidative Enzymes Leads to Reciprocal Inhibition |
title_full_unstemmed | Complex Formation between the Transcription Factor WRKY53 and Antioxidative Enzymes Leads to Reciprocal Inhibition |
title_short | Complex Formation between the Transcription Factor WRKY53 and Antioxidative Enzymes Leads to Reciprocal Inhibition |
title_sort | complex formation between the transcription factor wrky53 and antioxidative enzymes leads to reciprocal inhibition |
topic | catalase (CAT) ascorbate peroxidase (APX) superoxide dismutase (SOD) WRKY transcription factors WRKY53 protein–protein interaction |
url | https://www.mdpi.com/2076-3921/13/3/315 |
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