Plants contain three thioredoxin systems. Chloroplast thioredoxins are reduced by ferredoxin-thioredoxin reductase, whereas the cytosolic and mitochondrial thioredoxins are reduced by NADPH thioredoxin reductase (NTR). There is high similarity among NTRs from plants, lower eukaryotes, and bacteria, which are different from mammal NTR. Here we describe the OsNTRC gene from rice encoding a novel NTR with a thioredoxin-like domain at the C terminus, hence, a putative NTR/thioredoxin system in a single polypeptide. Orthologous genes were found in other plants and cyanobacteria, but not in bacteria, yeast, or mammals. Full-length OsNTRC and constructs with truncated NTR and thioredoxin domains were expressed in Escherichia coli as His-tagged polypeptides, and a polyclonal antibody specifically cross-reacting with the OsNTRC enzyme was raised. An in vitro activity assay showed that OsNTRC is a bifunctional enzyme with both NTR and thioredoxin activity but is not an NTR/thioredoxin system. Although the OsNTRC gene was expressed in roots and shoots of rice seedlings, the protein was exclusively found in shoots and mature leaves. Moreover, fractionation experiments showed that OsNTRC is localized to the chloroplast. An Arabidopsis NTRC knock-out mutant showed growth inhibition and hypersensitivity to methyl viologen, drought, and salt stress. These results suggest that the NTRC gene is involved in plant protection against oxidative stress.

The sessile nature of plants forces them to face an ever-changing environment instead of escape from hostile conditions as animals do. In order to overcome this survival challenge, a fine monitoring and controlling of the status of the photosynthetic electron transport chain (PETC) and the general metabolism is vital for these organisms. Frequently, evolutionary plant adaptation has consisted in the appearance of multigenic families, comprising an array of enzymes, structural components, or sensing and signaling elements, in numerous occasions with highly conserved primary sequences that sometimes make it difficult to discern between redundancy and specificity among the members of a same family. However, all this gene diversity is aimed to sort environment-derived plant signals to efficiently channel the external incoming information inducing a right physiological answer. Oxygenic photosynthesis is a powerful source of reactive oxygen species (ROS), molecules with a dual oxidative/signaling nature. In response to ROS, one of the most frequent post-translational modifications occurring in redox signaling proteins is the formation of disulfide bridges (from Cys oxidation). This review is focused on the role of plastid thioredoxins (pTRXs), proteins containing two Cys in their active site and largely known as part of the plant redox-signaling network. Several pTRXs types have been described so far, namely, TRX f, m, x, y, and z. In recent years, improvements in proteomic techniques and the study of loss-of-function mutants have enabled us to grasp the importance of TRXs for the plastid physiology. We will analyze the specific signaling function of each TRX type and discuss about the emerging role in non-photosynthetic plastids of these redox switchers.

In this study, evidence is provided for the role of fructose-1,6-bisphosphatases (FBPases) in plant development and carbohydrate synthesis and distribution by analysing two Arabidopsis thaliana T-DNA knockout mutant lines, cyfbp and cfbp1, and one double mutant cyfbp cfbp1 which affect each FBPase isoform, cytosolic and chloroplastic, respectively. cyFBP is involved in sucrose synthesis, whilst cFBP1 is a key enzyme in the Calvin–Benson cycle. In addition to the smaller rosette size and lower rate of photosynthesis, the lack of cFBP1 in the mutants cfbp1 and cyfbp cfbp1 leads to a lower content of soluble sugars, less starch accumulation, and a greater superoxide dismutase (SOD) activity. The mutants also had some developmental alterations, including stomatal opening defects and increased numbers of root vascular layers. Complementation also confirmed that the mutant phenotypes were caused by disruption of the cFBP1 gene. cyfbp mutant plants without cyFBP showed a higher starch content in the chloroplasts, but this did not greatly affect the phenotype. Notably, the sucrose content in cyfbp was close to that found in the wild type. The cyfbp cfbp1 double mutant displayed features of both parental lines but had the cfbp1 phenotype. All the mutants accumulated fructose-1,6-bisphosphate and triose-phosphate during the light period. These results prove that while the lack of cFBP1 induces important changes in a wide range of metabolites such as amino acids, sugars, and organic acids, the lack of cyFBP activity in Arabidopsis essentially provokes a carbon metabolism imbalance which does not compromise the viability of the double mutant cyfbp cfbp1.

NADPH thioredoxin reductase C plays a pivotal role required for the function of Trxs x and f and is essential for early seedling development.