The acceleration of climate change is necessitating the adoption of shifts in farming practices and technology to ensure the sustainability of agricultural production and food security. Because abiotic stresses such as drought and chilling represent major constraints on agricultural productivity worldwide, in this study, the mitigation of such stresses by the fungus Trichoderma asperellum HK703 was evaluated. The fungus was grown on whole grain oats, kaolin and vermiculite for 5 days and then the formulation was mixed with the potting soil to colonize the roots of the plants. The effect of the bioinoculant on tomato under drought or chilling was analyzed in tomato (Solanum lycopersicum) plants. Leaf, stem and root succulence, electrolyte leakage, the relative growth rate of plant height, stem thickness and leaf area, as well new leaf emergence and chlorophyll content were determined. The results showed that drought or chilling increased electrolyte leakage and reduced plant growth and development traits and chlorophyll (a,b) content. However, inoculation with T. asperellum eliminated or reduced most of the negative impacts of drought compared to the non-stressed plants, with the exception of chlorophyll b content. Furthermore, inoculation with T. asperellum improved some of the evaluated features in chilling stressed plants but had no effect on plant height or chlorophyll (a,b) content. The results of this study indicate that T. asperellum was more effective in alleviating drought than chilling stress in tomato plants.

NaTrxh, a thioredoxin type h, shows differential expression between self-incompatible and self-compatible Nicotiana species. NaTrxh interacts in vitro with S-RNase and co-localizes with it in the extracellular matrix of the stylar transmitting tissue. NaTrxh contains N- and C-terminal extensions, a feature shared by thioredoxin h proteins of subgroup 2. To ascertain the function of these extensions in NaTrxh secretion and protein-protein interaction, we performed a deletion analysis on NaTrxh and fused the resulting variants to GFP.

Soluble secretory proteins with a signal peptide reach the extracellular space through the endoplasmic reticulum-Golgi conventional pathway. During translation, the signal peptide is recognised by the signal recognition particle and results in a co-translational translocation to the endoplasmic reticulum to continue the secretory pathway. However, soluble secretory proteins lacking a signal peptide are also abundant, and several unconventional (endoplasmic reticulum/Golgi independent) pathways have been proposed and some demonstrated. This work describes new features of the secretion signal called Nβ, originally identified in NaTrxh, a plant extracellular thioredoxin, that does not possess an orthodox signal peptide. We provide evidence that other proteins, including thioredoxins type h, with similar sequences are also signal peptide-lacking secretory proteins. To be a secretion signal, positions 5, 8 and 9 must contain neutral residues in plant proteins–a negative residue in position 8 is suggested in animal proteins–to maintain the Nβ motif negatively charged and a hydrophilic profile. Moreover, our results suggest that the NaTrxh translocation to the endoplasmic reticulum occurs as a post-translational event. Finally, the Nβ motif sequence at the N- or C-terminus could be a feature that may help to predict protein localisation, mainly in plant and animal proteins.

Soluble secretory proteins with a signal peptide reach the extracellular space through the endoplasmic reticulum-Golgi conventional pathway. During translation, the signal peptide is recognised by the secretory recognition particle and results in a co-translational translocation to the endoplasmic reticulum to continue the secretory pathway. However, soluble secretory proteins lacking a signal peptide are also abundant, and several unconventional (endoplasmic reticulum/Golgi independent) pathways have been proposed and some demonstrated. This work describes new features of the secretion signal called Nβ, originally identified in NaTrxh, a plant extracellular thioredoxin, that does not possess an orthodox signal peptide. We provide evidence that other proteins, including thioredoxins type h , with similar sequences are also signal peptide-lacking secretory proteins. To be a secretion signal, positions 5, 8 and 9 must contain neutral residues –a negative residue in position 9 in animal proteins– to maintain the Nβ motif negatively charged and a hydrophilic profile. Moreover, our results suggest that the NaTrxh translocation to the endoplasmic reticulum occurs as a post-translational event. Finally, the Nβ motif sequence at the N- or C-terminus could be a feature that may help to predict protein localisation, mainly in plant and animal proteins.