"A cell wall surrounds every cell in a plant. It supports and determines the plant¿s physical form and provides a barrier against invading pathogens. The wall polysaccharides are synthesized by glycosyltransferases (GTs) located in the Golgi vesicles. Char acteristic signature structures for Golgi targeting have not been defined and this raises a question as to how the targeting of the GTs occurs. Many Golgi enzymes are known to be targeted by interactions with other proteins. We reason that this could be pa rticularly true for enzymes involved in biosynthesis of complex polysaccharides, which are likely to be synthesized by protein complexes. The objective is to identify the mechanism for Golgi targeting of the GTs from the perspective of protein-protein inte raction. This targeting will be investigated using fluorescent fusion proteins and confocal laser scanning microscopy. Direct protein-protein interactions will be elucidated by comparing targeting in wild type background and in mutants lacking components o f the biosynthetic machinery as well as by fluorescence resonance energy transfer (FRET). Invading bacterial pathogens interact with the cell wall and in some instances form biofilm. Therefore, cell wall components, particularly the polysaccharide struc tures and oligosaccharides derived from these, may be important stimuli in this context. GT mutants will be analyzed for their susceptibility to bacterial attachment, biofilm formation, and subsequent disease development. Because microbial biofilm is a con tinuing problem in both medical and industrial settings, the results have potential for technological applications, such as for designing coating materials for medical devices and in the food industry. The specific scientific goals are: - To identify novel Golgi proteins interacting with known GTs. - To investigate protein-protein interactions in vivo in the Golgi apparatus. - To evaluate plant polysaccharides as substrates or inducers of microbial biofilm"
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