The Phosphofructokinase Isoform AtPFK5 Is a Novel Target of Plastidic Thioredoxin-f-Dependent Redox Regulation
The chloroplast primary metabolism is of central importance for plant growth and performance. Therefore, it is tightly regulated in order to adequately respond to multiple environmental conditions. A major fluctuation that plants experience each day is the change between day and night, i.e., the cha...
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| Format: | Article |
| Language: | English |
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MDPI AG
2021-03-01
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| Series: | Antioxidants |
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| Online Access: | https://www.mdpi.com/2076-3921/10/3/401 |
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| author | Natalia Hess Simon Richter Michael Liebthal Karl-Josef Dietz Angelika Mustroph |
| author_facet | Natalia Hess Simon Richter Michael Liebthal Karl-Josef Dietz Angelika Mustroph |
| author_sort | Natalia Hess |
| collection | DOAJ |
| description | The chloroplast primary metabolism is of central importance for plant growth and performance. Therefore, it is tightly regulated in order to adequately respond to multiple environmental conditions. A major fluctuation that plants experience each day is the change between day and night, i.e., the change between assimilation and dissimilation. Among other mechanisms, thioredoxin-mediated redox regulation is an important component of the regulation of plastid-localized metabolic enzymes. While assimilatory processes such as the Calvin–Benson cycle are activated under illumination, i.e., under reducing conditions, carbohydrate degradation is switched off during the day. Previous analyses have identified enzymes of the oxidative pentose phosphate pathway to be inactivated by reduction through thioredoxins. In this work, we present evidence that an enzyme of the plastidic glycolysis, the phosphofructokinase isoform AtPFK5, is also inactivated through reduction by thioredoxins, namely by thioredoxin-f. With the help of chemical oxidation, mutant analyses and further experiments, the highly conserved motif CXDXXC in AtPFK5 was identified as the target sequence for this regulatory mechanism. However, knocking out this isoform in plants had only very mild effects on plant growth and performance, indicating that the complex primary metabolism in plants can overcome a lack in AtPFK5 activity. |
| first_indexed | 2024-03-09T05:05:04Z |
| format | Article |
| id | doaj.art-691044e1cfb14c069c24b8565bd0a962 |
| institution | Directory Open Access Journal |
| issn | 2076-3921 |
| language | English |
| last_indexed | 2024-03-09T05:05:04Z |
| publishDate | 2021-03-01 |
| publisher | MDPI AG |
| record_format | Article |
| series | Antioxidants |
| spelling | doaj.art-691044e1cfb14c069c24b8565bd0a9622023-12-03T12:55:23ZengMDPI AGAntioxidants2076-39212021-03-0110340110.3390/antiox10030401The Phosphofructokinase Isoform AtPFK5 Is a Novel Target of Plastidic Thioredoxin-f-Dependent Redox RegulationNatalia Hess0Simon Richter1Michael Liebthal2Karl-Josef Dietz3Angelika Mustroph4Plant Physiology, University Bayreuth, Universitaetsstr. 30, 95440 Bayreuth, GermanyPlant Physiology, University Bayreuth, Universitaetsstr. 30, 95440 Bayreuth, GermanyDepartment of Biochemistry and Physiology of Plants, University of Bielefeld, 33615 Bielefeld, GermanyDepartment of Biochemistry and Physiology of Plants, University of Bielefeld, 33615 Bielefeld, GermanyPlant Physiology, University Bayreuth, Universitaetsstr. 30, 95440 Bayreuth, GermanyThe chloroplast primary metabolism is of central importance for plant growth and performance. Therefore, it is tightly regulated in order to adequately respond to multiple environmental conditions. A major fluctuation that plants experience each day is the change between day and night, i.e., the change between assimilation and dissimilation. Among other mechanisms, thioredoxin-mediated redox regulation is an important component of the regulation of plastid-localized metabolic enzymes. While assimilatory processes such as the Calvin–Benson cycle are activated under illumination, i.e., under reducing conditions, carbohydrate degradation is switched off during the day. Previous analyses have identified enzymes of the oxidative pentose phosphate pathway to be inactivated by reduction through thioredoxins. In this work, we present evidence that an enzyme of the plastidic glycolysis, the phosphofructokinase isoform AtPFK5, is also inactivated through reduction by thioredoxins, namely by thioredoxin-f. With the help of chemical oxidation, mutant analyses and further experiments, the highly conserved motif CXDXXC in AtPFK5 was identified as the target sequence for this regulatory mechanism. However, knocking out this isoform in plants had only very mild effects on plant growth and performance, indicating that the complex primary metabolism in plants can overcome a lack in AtPFK5 activity.https://www.mdpi.com/2076-3921/10/3/401phosphofructokinasethioredoxin<i>Arabidopsis thaliana</i>redox regulation |
| spellingShingle | Natalia Hess Simon Richter Michael Liebthal Karl-Josef Dietz Angelika Mustroph The Phosphofructokinase Isoform AtPFK5 Is a Novel Target of Plastidic Thioredoxin-f-Dependent Redox Regulation Antioxidants phosphofructokinase thioredoxin <i>Arabidopsis thaliana</i> redox regulation |
| title | The Phosphofructokinase Isoform AtPFK5 Is a Novel Target of Plastidic Thioredoxin-f-Dependent Redox Regulation |
| title_full | The Phosphofructokinase Isoform AtPFK5 Is a Novel Target of Plastidic Thioredoxin-f-Dependent Redox Regulation |
| title_fullStr | The Phosphofructokinase Isoform AtPFK5 Is a Novel Target of Plastidic Thioredoxin-f-Dependent Redox Regulation |
| title_full_unstemmed | The Phosphofructokinase Isoform AtPFK5 Is a Novel Target of Plastidic Thioredoxin-f-Dependent Redox Regulation |
| title_short | The Phosphofructokinase Isoform AtPFK5 Is a Novel Target of Plastidic Thioredoxin-f-Dependent Redox Regulation |
| title_sort | phosphofructokinase isoform atpfk5 is a novel target of plastidic thioredoxin f dependent redox regulation |
| topic | phosphofructokinase thioredoxin <i>Arabidopsis thaliana</i> redox regulation |
| url | https://www.mdpi.com/2076-3921/10/3/401 |
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