Abstract
Three types of related subcellular oil-rich particles are present in plants: storage oil bodies inseeds for gluconeogenesis during germination, storage oil bodies in pollen providing acyl moieties for membranesynthesis in the pollen tube, and tapetosomes in the anther tapetum for delivering lipids and proteins tothe maturing pollen surface. Each of these oil-rich particles has a basic structure of an oil body,which consists of a triacylglycerol matrix enclosed by a layer of phospholipids and the structuralprotein oleosins. All components of an oil body are synthesized and assembled in endoplasmic reticulum(ER), from which a budding oil body is released. An oleosin molecule has a highly conserved centraldomain of 72 uninterrupted hydrophobic residues flanked by variable amphipathic N-and C-terminal segments. Its unique central domain is presumed to haveevolved from a transmembrane segment of an ER protein. An oleosin molecule does not have an N-terminal ER-targeting signal and is targeted to the signal recognition particleand then ER via its central hydrophobic domain. Targeting studies of oleosin molecules that have been modifiedby adding a N-terminal ER-targeting signal, shortening the centralhydrophobic stretch and eliminating the N- or C-terminalamphipathic stretch, have provided a model delineating the mechanism of oleosin targeting to ER andoil bodies. A tapetosome possesses numerous oleosin-coated oil bodies associated ionically with abundantmembranous vesicles, both of which are assembled in and then detached from ER.
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Acknowledgments
The research was supported by the National Science Foundation (MCB-0131358) and the US Department of Agriculture (National Research Initiative Competitive Grant No. 2004-02429).
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Huang, A.H.C. (2006). Oleosins and Endoplasmic Reticulum in Seeds and Anthers. In: Robinson, D.G. (eds) The Plant Endoplasmic Reticulum. Plant Cell Monographs, vol 4. Springer, Berlin, Heidelberg. https://doi.org/10.1007/7089_057
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DOI: https://doi.org/10.1007/7089_057
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