Although phosphatidylinositol transfer proteins (PITPs) are known to serve critical functions in regulating a varied array of signal transduction processes in animals and yeast, the discovery of a similar class of proteins in plants occurred only recently. Here, we report the participation of Ssh1p, a soybean PITP-like protein, in the early events of osmosensory signal transduction in plants, a function not attributed previously to animal or yeast PITPs. Exposure of plant tissues to hyperosmotic stress led to the rapid phosphorylation of Ssh1p, a modification that decreased its ability to associate with membranes. An osmotic stress-activated Ssh1p kinase activity was detected in several plant species by presenting recombinant Ssh1p as a substrate in in-gel kinase assays. Elements of a similar osmosensory signaling pathway also were conserved in yeast, an observation that facilitated the identification of soybean protein kinases SPK1 and SPK2 as stress-activated Ssh1p kinases. This study reveals the activation of SPK1 and/or SPK2 and the subsequent phosphorylation of Ssh1p as two early successive events in a hyperosmotic stress-induced signaling cascade in plants. Furthermore, Ssh1p is shown to enhance the activities of a plant phosphatidylinositol 3-kinase and phosphatidylinositol 4-kinase, an observation that suggests that the ultimate function of Ssh1p in cellular signaling is to alter the plant's capacity to synthesize phosphoinositides during periods of hyperosmotic stress. INTRODUCTIONPhosphatidylinositol transfer proteins (PITPs) were identified originally by their ability to serve as diffusible carriers of phosphatidylinositol (PtdIns) and to a lesser extent phosphatidylcholine (PtdCho) from one distinct membrane compartment to another by using an in vitro assay (Wirtz, 1991). In recent years, several intriguing and critical biological roles beyond the transfer of phospholipids have been attributed to yeast and animal PITPs. The yeast PITP (Sec14p) is an essential protein that is required for cells to properly execute the formation of secretory vesicles from the Golgi complex (Bankaitis et al., 1990). A considerable body of evidence suggests that Sec14p serves as a "molecular sensor" to monitor and regulate the levels of PtdIns, PtdCho, and potentially diacylglycerol in the Golgi complex of yeast (Skinner et al., 1995;Kearns et al., 1997). In addition, Sec14p has been implicated in modulating the activity of a PtdIns 4-kinase that regulates protein secretion (Hama et al., 1999).An essential role for PITPs also is observed in mammals and Drosophila, in which the loss of PITP function leads to specific neurodegenerative diseases (Hamilton et al., 1997;Milligan et al., 1997). At the cellular level, the mammalian PITP is known to be required for inositol lipid signaling, secretory vesicle formation from the trans -Golgi network, and the fusion of secretory vesicles to the plasma membrane (Hay and Martin, 1993;Cunningham et al., 1995;Kauffmann-Zeh et al., 1995). Although yeast and animal PITPs are very similar...
, in the estimated aqueous volume of the guard-cell wall. The conclusion is that mannitol, a xenobiotic with structural similarity to sucrose, can move throughout the apoplast of a transpiring leaflet and accumulate in an osmotically significant concentration in the guard-cell wall. These data therefore provide support for a new role for sucrose as a signal metabolite that integrates essential functions of the whole leaf. In addition, the results raise questions about the physiological or experimental accumulation of other guard-cell-targeted apoplastic solutes such as plant growth regulators, particularly abscisic acid, and ions.
Palmitic acid is the major saturated fatty acid component of soybean [Glycine max (L.) Merr.] oil, typically accounting for approximately 11% of total seed oil content. Several genetic loci have been shown to control the seed palmitate content of soybean. One such locus, fap 2 , mediates an elevated seed palmitate phenotype. Previous biochemical studies indicated that the fap 2 locus is associated with a reduction in the activity of 3-keto-acyl-ACP synthase II (KAS II), an enzyme that initiates the elongation of palmitoyl-ACP to stearoyl-ACP in the plastid. The objective of the present research was to define the molecular basis by which the fap 2 locus increases seed palmitate levels. We isolated two closely related, yet unique KAS II cDNAs, designated GmKAS IIA and GmKAS IIB, from soybean cultivar Century (Fap 2 , Fap 2 ) and its derivative high palmitate germplasm C1727 (fap 2 , fap 2 ). The GmKAS IIB cDNAs recovered from Century and C1727 were identical. In contrast, a single base-pair substitution was found in the GmKAS IIA gene from C1727 versus Century which converted a tryptophan codon into a premature stop codon, a mutation that would be predicted to render the encoded enzyme nonfunctional. Knowledge of the DNA sequence polymorphism led to the development a facile, robust cleavage amplified polymorphic sequence (CAPS) marker that readily distinguishes the mutant GmKAS IIA gene. This marker faithfully associated with a second independent germplasm line bearing the fap 2 locus, and thus may be useful in breeding programs that target the development of high palmitate soybean cultivars.
Although phosphatidylinositol transfer proteins (PITPs) are known to serve critical functions in regulating a varied array of signal transduction processes in animals and yeast, the discovery of a similar class of proteins in plants occurred only recently. Here, we report the participation of Ssh1p, a soybean PITP-like protein, in the early events of osmosensory signal transduction in plants, a function not attributed previously to animal or yeast PITPs. Exposure of plant tissues to hyperosmotic stress led to the rapid phosphorylation of Ssh1p, a modification that decreased its ability to associate with membranes. An osmotic stress-activated Ssh1p kinase activity was detected in several plant species by presenting recombinant Ssh1p as a substrate in in-gel kinase assays. Elements of a similar osmosensory signaling pathway also were conserved in yeast, an observation that facilitated the identification of soybean protein kinases SPK1 and SPK2 as stress-activated Ssh1p kinases. This study reveals the activation of SPK1 and/or SPK2 and the subsequent phosphorylation of Ssh1p as two early successive events in a hyperosmotic stress-induced signaling cascade in plants. Furthermore, Ssh1p is shown to enhance the activities of a plant phosphatidylinositol 3-kinase and phosphatidylinositol 4-kinase, an observation that suggests that the ultimate function of Ssh1p in cellular signaling is to alter the plant's capacity to synthesize phosphoinositides during periods of hyperosmotic stress.
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