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The creosote bush (Larrea tridentata) is a xerophytic evergreen C3 shrub thriving in vast arid areas of North America. As the first step toward understanding the molecular mechanisms controlling the drought tolerance of this desert plant, we have isolated a dozen genes encoding transcription factors, including LtWRKY21 that encodes a protein of 314 amino acid residues. Transient expression studies with the GFP-LtWRKY21 fusion construct indicate that the LtWRKY21 protein is localized in the nucleus and is able to activate the promoter of an abscisic acid (ABA)-inducible gene, HVA22, in a dosage-dependent manner. The transactivating activity of LtWRKY21 relies on the C-terminal sequence containing the WRKY domain and a N-terminal motif that is essential for the repression activity of some regulators in ethylene signaling. LtWRKY21 interacts synergistically with ABA and transcriptional activators VP1 and ABI5 to control the expression of the HVA22 promoter. Co-expression of VP1, ABI5, and LtWRKY21 leads to a much higher expression of the HVA22 promoter than does the ABA treatment alone. In contrast, the Lt-WRKY21-mediated transactivation is inhibited by two known negative regulators of ABA signaling: 1-butanol, an inhibitor of phospholipase D, and abi1-1, a dominant negative mutant protein phosphatase. Interestingly, abi1-1 does not block the synergistic effect of LtWRKY21, VP1, and ABI5 co-expression, indicating that LtWRKY21, VP1, and ABI5 may form a complex that functions downstream of ABI1 to control ABA-regulated expression of genes.The phytohormone abscisic acid (ABA) 1 modulates plant developmental processes such as seed formation, dormancy, and germination, as well as plant responses to environmental stresses such as drought, cold, high salinity, pathogen attack, and UV radiation (1-6). Plant responses to ABA are mediated at several molecular levels including transcription, RNA processing, post-translational modification, and metabolism of the secondary messengers (reviewed in Refs. 5-7). Recent data indicate that the ABA signaling pathways appear to be conserved among higher plant species and even bryophytes (8, 9).Both ABA-resistant and ABA-hypersensitive mutants have been extremely valuable in helping define ABA signaling pathways. Studies of mutants in several plant species suggest that the ABA signaling is mediated by a membrane-bound metal sensor (10, 11), type 2C serine/threonine protein phosphatases (12-14), a Ser/Thr protein kinase (15, 16), a protein farnesyl transferase (17), a steroid reductase (16), an inositol polyphosphate 1-phosphatase (18), and several transcription factors (19 -26). In addition, the mutant studies also suggest that RNA processing plays an important role in the regulation of ABA signaling (27) because several ABA response mutants are impaired in a double-stranded RNA-binding protein (28), a mRNA CAP-binding protein (29), or a U6-related Sm-like small ribonucleoprotein (18). In line with these reports, an ABA-induced maize glycine-rich protein can bind to uridine-and guanosi...

Gibberellins (GAs) regulate many aspects of plant development, such as germination, growth, and flowering. The barley (Hordeum vulgare) Amy32b a-amylase promoter contains at least five cis-acting elements that govern its GA-induced expression. Our previous studies indicate that a barley WRKY gene, HvWRKY38, and its rice (Oryza sativa) ortholog, OsWRKY71, block GA-induced expression of Amy32b-GUS. In this work, we investigated the functional and physical interactions of HvWRKY38 with another repressor and two activators in barley. HvWRKY38 blocks the inductive activities of SAD (a DOF protein) and HvGAMYB (a R2R3 MYB protein) when either of these proteins is present individually. However, SAD and HvGAMYB together overcome the inhibitory effect of HvWRKY38. Yet, the combination of HvWRKY38 and BPBF (another DOF protein) almost diminishes the synergistic effect of SAD and HvGAMYB transcriptional activators. Electrophoretic mobility shift assays indicate that HvWRKY38 blocks the GA-induced expression of Amy32b by interfering with the binding of HvGAMYB to the cis-acting elements in the a-amylase promoter. The physical interaction of HvWRKY38 and BPBF repressors is demonstrated via bimolecular fluorescence complementation assays. These data suggest that the expression of Amy32b is modulated by protein complexes that contain either activators (e.g. HvGAMYB and SAD) or repressors (e.g. HvWRKY38 and BPBF). The relative amounts of the repressor or activator complexes binding to the Amy32b promoter regulate its expression level in barley aleurone cells.

Rotaviruses were detected by an ELISA test in stool specimens from diarrheic rabbits in two commercial rabbitries and cultured in MA 104 cells. Their identity was confirmed by electron microscopy and indirect immunofluorescence. They were found to belong to subgroup I by testing with monoclonal antibodies and to serotype 3 by neutralization with homologous and heterologous antisera. Although both viruses were neutralized by antiserum to human serotype 3 the ALA rabbit rotavirus was minimally neutralized by antiserum to the C11 rabbit rotavirus. Electrophoresis of viral RNA revealed 11 segments characteristic of rotavirus, however both rabbit rotaviruses had unusual electropherotypes. They differed from each other with greatly reduced mobility of the tenth segment in one virus and the eleventh segment in the other virus.