Generation of transgenic wheat (Triticum aestivum L.) accumulating heterologous endo-xylanase or ferulic acid esterase in the endosperm.

Endo-xylanase (from Bacillus subtilis) or ferulic acid esterase (from Aspergillus niger) were expressed in wheat under the control of the endosperm-specific 1DX5 glutenin promoter. Constructs both with and without the endoplasmic reticulum retention signal (Lys-Asp-Glu-Leu) KDEL were used. Transgenic plants were recovered in all four cases but no qualitative differences could be observed whether KDEL was added or not.

Solubilization of an arabinan arabinosyltransferase activity from mung bean hypocotyls.

The biosynthesis of polysaccharides destined for the plant cell wall and the subsequent assembly of the cell wall are poorly understood processes that are currently the focus of much research. Arabinan, a component of the pectic polysaccharide rhamnogalacturonan I, is composed of arabinosyl residues connected via various glycosidic linkages, and therefore, the biosynthesis of arabinan is likely to involve more than one arabinosyltransferase. We have studied the transfer of [(14)C]arabinose (Ara) from UDP-L-arabinopyranose onto polysaccharides using microsomal membranes isolated from mung bean (Vigna radiata) hypocotyls.

Expression patterns of cell wall-modifying enzymes during grape berry development.

During ripening of grape (Vitis vinifera L.) berries, softening occurs concomitantly with the second growth phase of the fruit and involves significant changes in the properties of cell wall polysaccharides. Here, the activities of enzymes that might participate in cell wall modification have been monitored throughout berry development.

Definition of a minimal munc18c domain that interacts with syntaxin 4.

munc18c is a critical protein involved in trafficking events associated with syntaxin 4 and which also mediates inhibitory effects on vesicle docking and/or fusion. To investigate the domains of munc18c responsible for its interaction with syntaxin 4, fragments of munc18c were generated and their interaction with syntaxin 4 examined in vivo by the yeast two-hybrid assay. In vitro protein-protein interaction studies were then used to confirm that the interaction between the proteins was direct.

Enzymatic synthesis and purification of uridine diphospho-beta-l-arabinopyranose, a substrate for the biosynthesis of plant polysaccharides.

Many plant cell wall components such as the polysaccharides xylans and pectins or the glycoproteins arabinogalactan proteins and extensins contain arabinosyl residues. The arabinosyl substituents are thought to be incorporated into these wall polymers by the action of arabinosyltransferases using UDP-l-arabinose as the precursor. UDP-l-arabinose is not commercially available and therefore a procedure for generating UDP-l-arabinose was developed for use in studies on the biosynthesis of the arabinose-containing polymers.