Two soybean cDNA clones, SPK-3 and SPK-4, encoding putative protein kinases were isolated and characterized. Both cDNAs encoded approximately 40-kDa serine/threonine kinases with unusual stretches of acidic amino acids in their carboxy-terminal regions, which are highly homologous to PKABA1 from wheat and ASKs from Arabidopsis. These kinases are encoded by one- or two-copy genes in the soybean genome. Notably, SPK-3 and -4 showed different patterns of expression in various soybean tissues. SPK-3 is highly expressed in dividing and elongating tissues of young seedlings but relatively weakly in tissues of mature plants. In contrast, SPK-4 showed relatively high and constitutive expression in all the tissues examined except for leaf tissues of mature plants. Although various stressors, such as dehydration and high salinity, increased the expression of both genes, the induction kinetics were different. The two genes also differed in their response to abscisic acid (ABA). SPK-3 was induced but SPK-4 was not affected by exogenously supplied abscisic acid. In accordance with these expression data analysis of the activity of a chimeric SPK-3 promoter::beta-glucuronidase (GUS) reporter gene by transient expression in tobacco leaves confirmed the inducibility of SPK-3 by salt and ABA. Polyclonal antibodies raised against a recombinant SPK-4 protein produced in Escherichia coli specifically recognized both recombinant SPK-3 and -4 proteins. Kinase assays using affinity-purified SPK-4/ antibody complexes with crude soybean extracts as substrate identified specific phosphorylation of two 41 and 170 kDa soybean proteins that were phosphorylated on serine residues. Taken together, our results suggest that SPK-3, and/or SPK-4 are functional serine protein kinase(s). Furthermore, SPK-3 and -4 may play different roles in the transduction of various environmental stresses.

The study about structure of Drosophila melanogaster's retinal cell using electron microscopy were carried in detail by Waddington and Perry [1][2]. But, these results can have limitation in cellular structure based upon studies of chemically prepared samples.Currently available freezing techniques by transmission electron microscopy are allowing the visualization of faithful representation of cell structures. The rapid freezing is so much better due to the speed of fixation, which freezing virtually means stopping all molecular movement [3][4]. In this study, the adult retina of Drosophila Melanogaster was investigated fixation by high pressure freezing and modified plunge freezing method followed freeze-substitution. Freeze-substitution was carried out in acetone (dried over calciumchloride) containing 2% osmiumtetroxid. The substitution was programmed as follows: 30 h at -90°C, heating at a rate of 5°C to -60°C, 8h -60°C, heating at a rate of 5°C to -30°C, 8h at -30°C, transfer of the samples to ice (0°C) for 1h, washing with acetone. Thereafter the samples were embedded in Epon-Araldite, ultrathin sectioned and poststained with uranylacetate and lead citrate. The current data provide us more precise cellular information and better understanding on the animal vision mechanism in new dimension.