The effect of salinity on plant available water

Salinity acts to inhibit plant access to soil water by increasing the osmotic strength of the soil solution. As the soil dries, the soil solution becomes increasingly concentrated, further limiting plant access to soil water. An experiment was conducted to examine the effect of salt on plant available water in a heavy clay soil, using a relatively salt tolerant species, wheat ‘Kennedy’, and a more salt sensitive species, chickpea ‘Jimbour’. Sodium chloride was applied to Red Ferrosol at 10 rates from 0 to 3 g/kg. Plants were initially maintained at field capacity. After 3 weeks, plants had become established and watering was ceased. The plants then grew using the water stored in the soil. Once permanent wilting point was reached plants were harvested, and soil water content was measured. The results showed that without salt stress, wheat and chickpea extracted approximately the same amount of water. However, as the salt concentration increased, the ability of chickpea to extract water was severely impaired, while wheat’s ability to extract water was not affected over the range of concentrations examined. Growth of both wheat and chickpea was reduced even from low salt concentrations. Possible explanations for this are that the effect on growth is due to Cl- toxicity and that this occurs at lower concentrations than the osmotic effect of salinity, or that the metabolic demands of maintaining plant water balance and extracting soil water under saline conditions result in reduced growth.

Structural and functional characterization of the conserved salt bridge in mammalian Paneth cell alpha-defensins - Solution structures of mouse cryptdin-4 AND (E15D)-cryptdin-4

Defensins are mediators of mammalian innate immunity, and knowledge of their structure-function relationships is essential for understanding their mechanisms of action. We report here the NMR solution structures of the mouse Paneth cell α-defensin cryptdin-4 (Crp4) and a mutant (E15D)-Crp4 peptide, in which a conserved Glu15 residue was replaced by Asp. Structural analysis of the two peptides confirms the involvement of this Glu in a conserved salt bridge that is removed in the mutant because of the shortened side chain. Despite disruption of this structural feature, the peptide variant retains a well defined native fold because of a rearrangement of side chains, which result in compensating favorable interactions. Furthermore, salt bridge-deficient Crp4 mutants were tested for bactericidal effects and resistance to proteolytic degradation, and all of the variants had similar bactericidal activities and stability to proteolysis. These findings support the conclusion that the function of the conserved salt bridge in Crp4 is not linked to bactericidal activity or proteolytic stability of the mature peptide.