One possible explanation for the molecular and physiological LY2109761 phenotype of atx-3 nulls is that the absence of ataxin-3 at some timepoint of the development causes cellular stress, which activates the stress machinery, and once they are needed again, chaperones and other effectors will be more effectively and rapidly activated- a process known as hormesis. Another possibility is that ataxin-3 is normally regulating chaperone levels via the DAF-16 pathway, or even modulating their levels through the ubiquitin-proteasome degradation of a specific target upstream DAF-16 or of DAF-16 itself. This last option seems unlikely as we did not find significant differences in DAF-16 protein levels in atx- 3 mutant animals, in agreement with very recent findings. In summary, we show that the absence of ataxin-3 leads to an enhanced stress response in C. elegans. This phenotype was correlated with a significant increase in chaperones and fully dependent on the transcription factorDAF-16 and on its target HSP-16.2, and on the hsp70-like C12C8.1 chaperone.These findings can be relevant in the disease context, since a partial loss of the normal function of ataxin-3 may occurdue to the expansion, as has been observed for other polyQ disorders. Long-term deregulation of HSPscan be detrimental for cell growth, division and viability and, along with the proteotoxic stress, this may contribute to neuronal demise in the context of MJD. Plants are sessile organisms that are continually challenged by microbial pathogens during their life cycle. To ward off pathogen attack, plants produce a number of cationic antimicrobial peptides. These include defensins that are one of the largest families of antimicrobial peptides found in plants. These basic, cysteine-rich, proteins are 45 to 54 amino acids in length and share significant structural homology with defensins from insects, mollusks and mammals. All plant defensins contain an invariant tetradisulfide array and share a common cysteinestablized a/b structure composed of three antiparallel bstrands and one a-helix. Despite their structural similarity, the amino acid sequences of plant defensins are highly diverse. This variation in primary sequences may account for different functions attributed to plant defensins including antibacterial activity, zinc tolerance, proteinase and a-amylase inhibitory activity, ion channel blocking activity as well as pollen tube growth arrest, burst and sperm discharge. A large number of cationic plant defensins exhibit inhibitory activity PCI-32765 Src-bcr-Abl inhibitor against filamentous fungi in vitro and in transgenic plants. Because of their potent in vitro antifungal activity, plant defensins have the potential to be used as antifungal agents in transgenic crops. A growing body of evidence suggests that plant defensins with highly diverse primary structures inhibit the growth of target fungi via different modes of action.