We would be able to analyze the Ruxolitinib effects of Arp8 expression level on genome stability and would also be able to analyze functions of Arp8 mutants in the absence of endogenous Arp8. This system will provide further knowledge on the roles of Arp8 and INO80 complex in epigenetic regulations including DNA repair and transcription. Some organisms can survive the almost total loss of their cellular water in a process that is called anhydrobiosis. The most common anhydrobiotes are found in higher plants, since in most species, orthodox seeds acquire desiccation tolerance during maturation. Once shed as dry and quiescent organisms, seeds can be stored for very long periods before resuming life during imbibition, and rapidly germinate. Considering the constraint imposed by desiccation to biological structures and components, it is not surprising that specific proteins are expressed in the context of anhydrobiosis. LEAPs were originally discovered in Gossypium hirsutum seeds. LEAPs have been also identified in bacteria, fungi, algae and animals and are associated with abiotic stress tolerance, particularly dehydration, cold stress and salt stress, suggesting a general protective role in anhydrobiotic organisms. Most of LEAPs are intrinsically disordered proteins and thus little is known about their molecular mechanism of action, although in vitro assays with various LEAPs suggested roles in desiccation and/or freezing aggregation, or membrane protection. For example, in vitro experiments have shown that in the hydrated state, mitochondrial LEAP is unfolded and does not hamper mitochondrial functioning, while in the dry state, it folds and enters the inner membrane to provide protection. LEAPs were also shown to sequester calcium, metal ions and reactive oxygen species and to contribute to the glassy state. However, despite their role in membrane protection and some theoretical studies such as molecular dynamics simulations the actual functional mechanism of LEAPs at the molecular level remains to be demonstrated for most of them. Investigating the structure – function relationships of LEAPs is thus of primary interest, but remains challenging because experimental evidence is difficult to obtain. Since LEAPs were early recognized as highly hydrophilic proteins, this led Garay-Arroyo et al. to propose they were members of a more widespread group of proteins, which they coined hydrophilin, characterized by a high glycine content and high average hydrophilicity. Interestingly, in yeast and Escherichia coli, hydrophilins expression appeared well correlated with osmotic stress, and the yeast hydrophilin STF2p was found to be essential for dehydration tolerance. In a further analysis, in which the Gly criteria for hydrophilins was lowered to 6%, Battaglia et al. concluded that LEAPs were indeed hydrophilins since 92% of 378 LEAPs fulfilled a high Gly content and a low hydrophobicity. Water stress and hypersensitive response domain is a region of unknown function found in several plant proteins involved in either the response to water stress or the response to bacterial infection. WHy domain is also found in several bacterial and archaeal proteins whose functions are not currently known.