Milla M.A.R.Townsend J.Chang I.-F.Cushman J.C.2019-07-172019-07-17200601674412https://scholars.lib.ntu.edu.tw/handle/123456789/414140The AtDi19 (drought-induced) gene family encodes seven hydrophilic proteins that contain two atypical Cys2/His2 (C2H2) zinc finger-like domains that are evolutionarily well-conserved within angiosperms suggesting a conserved and important function. Five of the seven Arabidopsis AtDi19-related:DsRed2 fusion proteins exhibited speckled patterns of localization within the nucleus as shown by transient expression analysis in Arabidopsis protoplasts. In contrast, AtDi19-2:DsRed2 was present in the nucleus and cytoplasm, whereas AtDi19-4:DsRed2 was localized to the nuclear periphery. mRNA expression studies showed that AtDi19 genes are ubiquitously expressed in Arabidopsis tissues, although some differences were observed. In seedlings, RT-PCR analyses showed that AtDi19-1 and AtDi19-3 steady-state transcript amounts were rapidly induced by dehydration, whereas transcript amounts for AtDi19-2 and AtDi19-4 increased in response to high-salt stress. In addition, the mRNA abundance of all the AtDi19-related gene family members was not regulated by ABA. These data, taken together, suggest that several AtDi19-related gene family members may function in ABA-independent, dehydration and salinity stress signaling pathways. However, they may also be regulated by other abiotic stimuli. AtDi19-7, for example, has been implicated in regulating light signaling and responses. Finally, we show that most AtDi19-related proteins are phosphorylated in vitro by calcium-dependent protein kinases suggesting that this post-translational modification may be important for regulating the function of this novel protein family. ? Springer 2006.Abiotic stressNucleusPhosphorylationProtein familyZinc fingerThe arabidopsis AtDi19 gene family encodes a novel type of Cys2/His2 zinc-finger protein implicated in ABA-independent dehydration, high-salinity stress and light signaling pathwaysjournal article10.1007/s11103-005-5798-72-s2.0-33745193104https://www.scopus.com/inward/record.uri?eid=2-s2.0-33745193104&doi=10.1007%2fs11103-005-5798-7&partnerID=40&md5=dc1c74bc0b4271d823bea781950c2c31