Journal
ANTIOXIDANTS
Volume 10, Issue 3, Pages -Publisher
MDPI
DOI: 10.3390/antiox10030401
Keywords
phosphofructokinase; thioredoxin; Arabidopsis thaliana; redox regulation
Funding
- Stifterverband fur die Deutsche Wissenschaft [H140 5409 9999 15625]
- German Research Foundation (DFG)
- University of Bayreuth
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The chloroplast primary metabolism is tightly regulated to respond to various environmental conditions, including daily changes between day and night. Thioredoxin-mediated redox regulation is a crucial component in regulating plastid-localized metabolic enzymes, ensuring proper assimilation and dissimilation processes in plants.
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.
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