Characterization of Clathrin Coated Vesicles Involved in Transport of Vacuolar Proteins in Plants

点击翻译按钮获取中文摘要

Developing pea cotyledons are sites of synthesis of specific reserve proteins. The synthesis of these proteins is developmentally regulated and tissue specific. Within the parenchyma cells of the developing pea cotyledons the reserve proteins accumulate in sub-cellular organelles termed protein bodies which arise by sub-division of the large central vacuole originally present in the cells. The reserve proteins are synthesized on the rough endoplasmic reticulum and pass through the Golgi. This laboratory has established that the transport of the reserve protein lectin and other vacuolar hydrolases from the Golgi involves clathrin coated visicles. To date only limited information is available on the biochemistry and function of coated vesicles in plant systems. The proposed research will capitalize on the rich source of coated vesicles present in developing pea cotyledons to conduct a detailed study of aspects of their biochemistry and function. The immediate aims of this research are to characterize the clathrin light chain which has only recently been identified in plants. The primary sequences of the light chain peptides will be determined and the mechanism of their interaction with the heavy chain establshed. Kinase activities will be assayed in the coated vesicles from developing peas to determine whether, in similarity to animal systems, the light chain peptide is phosphroylated. The results of these studies will contribute to our knowledge of the biology of plant cells and will enhance our understanding of the selectivity of intracellular protein transport.