caa a22 4500 467894582 CHVBK 20180406152759.0 cr unu---uuuuu 170328e20060501xx s 000 0 eng 10.1007/s11103-005-5798-7 doi (NATIONALLICENCE)springer-10.1007/s11103-005-5798-7 The 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 Pathways [Elektronische Daten] [Miguel Milla, Jared Townsend, Ing-Feng Chang, John Cushman] The 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 stress nationallicence nucleus nationallicence phosphorylation nationallicence protein family nationallicence zinc finger nationallicence ABA : abscisic acid nationallicence ACN : acetonitrile nationallicence AP2 : APETALA2 nationallicence ATP : adenosine triphosphate nationallicence BSA : bovine serum albumin nationallicence CBF : C-repeat binding factor nationallicence Di : drought-induced nationallicence DREB : DRE binding protein nationallicence DTT : dithiolthreitol nationallicence EST : expressed sequence tag nationallicence HEPES : N-2-hydroxyethyl piperazine-N′-2-ethane sulfonic acid nationallicence IPTG : isopropyl-beta-d-thiogalactopyranoside nationallicence ORF : open reading frame nationallicence MALDI-TOF : matrix-assisted laser desorption ionization-time-of-flight nationallicence MES : morpholinoethane sulfonic acid nationallicence MS : mass spectrometry nationallicence NCBI : National Center for Biotechnology Information nationallicence NLS : nuclear localization signal nationallicence PEG : polyethylene glycol nationallicence PVP : polyvinylpyrollidone nationallicence RT-PCR : reverse transcription-polymerase chain reaction nationallicence SDS-PAGE : sodium dodecyl sulfate-polyacrylamide gel electrophoresis nationallicence TFA : trifluoroacetic acid nationallicence Milla Miguel Department of Biochemistry and Molecular Biology, University of Nevada, 89557-0014, Reno, NV, USA aut Townsend Jared Department of Biochemistry and Molecular Biology, University of Nevada, 89557-0014, Reno, NV, USA aut Chang Ing-Feng Department of Biochemistry and Molecular Biology, University of Nevada, 89557-0014, Reno, NV, USA aut Cushman John Department of Biochemistry and Molecular Biology, University of Nevada, 89557-0014, Reno, NV, USA aut Plant Molecular Biology Kluwer Academic Publishers 61/1-2(2006-05-01), 13-30 0167-4412 61:1-2<13 2006 61 11103 https://doi.org/10.1007/s11103-005-5798-7 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11103-005-5798-7 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Milla Miguel Department of Biochemistry and Molecular Biology, University of Nevada, 89557-0014, Reno, NV, USA aut NATIONALLICENCE 700 1- Townsend Jared Department of Biochemistry and Molecular Biology, University of Nevada, 89557-0014, Reno, NV, USA aut NATIONALLICENCE 700 1- Chang Ing-Feng Department of Biochemistry and Molecular Biology, University of Nevada, 89557-0014, Reno, NV, USA aut NATIONALLICENCE 700 1- Cushman John Department of Biochemistry and Molecular Biology, University of Nevada, 89557-0014, Reno, NV, USA aut NATIONALLICENCE 773 0- Plant Molecular Biology Kluwer Academic Publishers 61/1-2(2006-05-01), 13-30 0167-4412 61:1-2<13 2006 61 11103 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer