AI Article Synopsis
- Plants have three types of NADPH-thioredoxin reductases (NTRs) that play key roles in their metabolism, but the impact of mutants lacking all three had not been fully explored.
- Researchers created and studied triple and double mutants in Arabidopsis to see how they respond to different environmental conditions.
- The results showed that while the mutants had reduced growth and metabolic changes, the triple mutant exhibited unique interactions between chloroplastic and extra-chloroplastic NTRs, particularly in photosynthesis under varying light and CO levels, suggesting other redox mechanisms can partially compensate for the loss of NTR function.
Article Abstract
Plants contain three NADPH-thioredoxin reductases (NTR) located in the cytosol/mitochondria (NTRA/B) and the plastid (NTRC) with important metabolic functions. However, mutants deficient in all NTRs remained to be investigated. Here, we generated and characterised the triple Arabidopsis ntrabc mutant alongside with ntrc single and ntrab double mutants under different environmental conditions. Both ntrc and ntrabc mutants showed reduced growth and substantial metabolic alterations, especially in sink leaves and under high CO (HC), as compared to the wild type. However, ntrabc showed higher effective quantum yield of PSII under both constant and fluctuating light conditions, altered redox states of NADH/NAD and glutathione (GSH/GSSG) and lower potential quantum yield of PSII in sink leaves in ambient but not high CO concentrations, as compared to ntrc, suggesting a functional interaction between chloroplastic and extra-chloroplastic NTRs in photosynthesis regulation depending on leaf development and environmental conditions. Our results unveil a previously unknown role of the NTR system in regulating sink leaf metabolism and plant acclimation to HC, while it is not affecting full plant development, indicating that the lack of the NTR system can be compensated, at least to some extent, by other redox mechanisms.
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| http://dx.doi.org/10.1111/pce.14631 | DOI Listing |
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