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PLANT SEEDS: AN EXCITING MODEL SYSTEM FOR DISSECTING MOLECULAR AND CELLULAR REGULATION OF METABOLIC PROCESSES

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Metabolic processes are regulated by complex networks of interacting mechanisms that utilize various cellular machineries. Such complex networks may be well exemplified by the synthesis, accumulation, and degradation of storage proteins in developing and germinating seeds. Our laboratories are using plant seeds as a model system for studying the regulation of production of the essential amino acid lysine, the control of synthesis of storage proteins and their transport to the storage vacuoles, and the de novo formation of new forms of lytic vacuoles in germinating seeds which fuse with the storage vacuoles to enable degradation of the storage protein sand their mobilization into the germinating embryo. We show that: (i) production of lysine in developing seeds is regulated by complex pathways of synthesis and catabolism that involve the sensing of free lysine levels in the seeds, and (ii) analysis of the deposition of storage proteins in seed storage vacuoles and their subsequent degradation during germination provide novel insights into the biogenesis and function of vacuoles in plants.

Affiliations: 1: Department of Plant Sciences, The Weizmann Institute of Science, Rehovot 76100, Israel ; 2: MIGAL Galilee Technological Center, Kiryat Shmona, South Industrial Zone, Rosh Pina 12100, Israel ; 3: Climate Stress Laboratory USDA/ARS, Bldg. 006, Room 203, Beltsville, Maryland 20705, USA

10.1560/EEEP-KB7G-GGQH-5V0R
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1. Chrispeels, M., Higgins, T., and Spencer, D. 1982a. Assembly of storage protein oligomers in the endoplasmic reticulum and processing of the polypeptides in the protein bodies of developing pea cotyledons. J. Cell. Biol. 93: 306–313.
2. Kemper, E.L., Neto, G.C., Papes, F., Moraes, K.C., Leite, A., and Arruda, P. 1999. The role of Opaque2 in the control of lysine-degrading activities in developing maize endosperm. Plant Cell 11: 1981–1994.
3. Maurel, C. 1997. Aquaporins and water permeability of plant membranes. Annu. Rev. Plant Physiol. Plant Mol. Biol. 48: 399–429.
4. Gaziola, A., Teixeira, C.M.G., Lugli, J., Sodek, L., and Azevedo, R.A. 1997. The enzymology of lysine catabolism in rice seeds. Isolation, characterization, and regulatory properties of a lysine 2-oxoglutarate reductase/ saccharopine dehydrogenase bifunctional polypeptide. Eur. J. Biochem. 247: 364–371.
5. Goncalves-Butruille, M., Szajner, P., Torigoi, E., Leite, A., and Arruda, P. 1996. Purification of characterization of the bifunctional enzyme lysine-ketoglutarate reductasesaccharopine dehydrogenase from maize. Plant Physiol. 110: 765–771.
6. Okomoto, T., Minamikawa, T., Edward, G., Vakharia, V., and Herman, E.M. 1999. Posttranslational removal of the carboxyterminal KDEL of the cysteine protease SH-EP occurs prior to maturation of the enzyme. J. Biol. Chem. 274: 11390–11398.
7. Markovitz, P.J., Chuang, D.T., and Cox, R.P. 1984. Familial hyperlysinemias: purification and characterization of the bifunctional aminoadipic semialdehyde synthase with lysine-ketoglutarate reductase and saccharopine dehydrogenase activities. J. Biol. Chem. 259: 11643–11646.
8. Paris, N., Stanley, C.M., Jones, R.L., and Rogers, J.C. 1996. Plant cells contain two functionally distinct vacuolar compartments. Cell 85: 563–572.
9. Paris, N., Rogers, S., Jiang, L., Kirsch, T., Beevers, T., Phillips, T., and Rogers, J. 1997. Molecular cloning and further characterization of a probable plant vacuolar sorting receptor. Plant Physiol. 115: 29–39.
10. Schmid, M., Simpson, D., Kalousek, F., and Gietl, S. 1998. A cysteine endoprotease with a C-terminal KDEL motif isolated from castor bean endosperm is a marker enzyme for the ricinsome, a putative lytic compartment. Planta 206: 466–475.
11. Bollini, R. and Chrispeels, M. 1979. The rough endoplasmic reticulum is the site of reserve-protein synthesis in developing Phaseolus vulgaris cotyledons. Planta 146: 487– 501.
12. Chrispeels, M.J., Higgins, T.J.V., Craig, S., and Spencer, D. 1982b. Role of the endoplasmic reticulum in the synthesis of reserve proteins and the kinetics of their transport to protein bodies in developing pea cotyledons. J. Cell. Biol. 93: 5–14.
13. Tang, G., Zhu, X., Tang, X., and Galili, G. 2000. A novel composite locus of Arabidopsis encoding simulatenously two polypeptides with metabolically related but distinct functions in lysine catabolism. Plant J. 21: 1–10.
14. Baumgartner, B., Tokuyasu, K.T., and Chrispeels, M.J. 1978. Localization of vicilin peptidohydrolase in the cotyledons of mung bean seedlings by immunofluorescence microscopy. J. Cell. Biol. 79: 10–19.
15. Galili, G., Altschuler, Y., and Levanony, H. 1993. Assembly and transport of seed storage proteins. Trends Cell. Biol. 3: 437–443.
16. Levanony, H., Rubin, R., Altschuler, Y., and Galili, G. 1992. Evidence for a novel route of wheat storage proteins to vacuoles. J. Cell Biol. 119: 1117–1128.
17. Munro, S. and Pelham, H.R.B. 1987. A C-terminal signal prevents secretion of luminal ER proteins. Cell 48: 899–907.
18. Galili, G. and Herman, E.M. 1997. Protein bodies: storage vacuoles in seeds. Adv. Bot. Res. 25: 113–140.
19. Toyooka, K., Okamoto, T., and Minamikawa, T. 2000. Mass transport of proform of a KDEL-tailed proteinase (SH-EP) to protein storage vacuoles by ER-derived vesicle is involved in protein mobilization in germinating seeds. J. Cell. Biol. 148: 453–464.
20. Craig, S., Goodchild, D.J., and Hardham, A.R. 1979. Structural aspects of protein accumulation in developing pea cotyledons I. Qualitative and quantitative changes in parenchyma cell vacuoles. Aust. J. Plant Physiol. 6: 81–98.
21. Bollini, R., Vitale, A., Chrispeels, M.J. 1983. In vivo and in vitro processing of seed reserve protein in the endoplasmic reticulum: Evidence for two glycosylation steps. J. Cell. Biol. 96: 999–1007.
22. Johnson, K., Hofte, H., and Chrispeels, M. 1990. An intrinsic tonoplast protein of protein storage vacuoles in seeds is structurally related to a bacterial solute transporter (GlpF). Plant Cell 2: 525–532.
23. Coleman, C.E., Herman, E.M., Takasaki, K., and Larkins, B.A. 1996. The maize gamma-zein sequesters alpha-zein and stabilizes its accumulation in protein bodies of transgenic tobacco endosperm. Plant Cell 8: 2335–2345.
24. Karchi, H., Miron, D., Ben-Yaacov, S., and Galili, G. 1995. The lysine-dependent stimulation of lysine catabolism in tobacco seeds requires calcium and protein phosphorylation. Plant Cell 7: 1963–1970.
25. Ahmed, S.U., Bar-Peled, M., and Raikhel, N.V. 1997. Cloning and subcellular location of an Arabidopsis receptor-like protein that shares common features with protein-sorting receptors of eukaryotic cells. Plant Physiol. 114: 325–336.
26. Johnson, K.D., Herman, E.M., and Chrispeels, M.J. 1989. An abundant, highly-conserved tonoplast protein in seeds. Plant Physiol. 91: 1006–1013.
27. Swanson, S., Bethke, P., and Jones, R. 1998. Barley aleurone cells contain two types of vacuoles: characterization of lytic organelles by use of fluorescent probes. Plant Cell 10: 685–698.
28. Tang, G., Miron, D., Zhu-Shimoni, J.X., and Galili, G. 1997. Regulation of lysine catabolism through lysineketoglutarate reductase and saccharopine dehydrogenase in Arabidopsis. Plant Cell 9: 1–13.
29. Hara-Nishimura, I., Shimada, T., Hatano, K., Takeuchi, Y., and Nishimura, M. 1998. Transport of storage proteins to protein storage vacuoles is mediated by large precursor-accumulating vesicles. Plant Cell 10: 825–836.
30. Herman, E.M. and Larkins, B.A. 1999. Protein storage bodies and vacuoles. Plant Cell 11: 601–614.
31. Akasofu, H., Yamauchi, D., Mitsuhashi, W., and Minamikawa, T. 1989. Nucleotide sequence of cDNA for sulfhydrylendopeptidase (SH-EP) from cotyledons of germinating Vigna mungo seeds. Nucleic Acids Res 17: 6733.
32. Larkins, B.A. and Hurkman, W.J. 1978. Synthesis and deposition of zein in protein bodies of maize endosperm. Plant Physiol. 62: 256–263.
33. Miron, D., Ben-Yaacov, S., Reches, C., Schupper, A., and Galili, G. 2000. Purification and characterization of bifunctional lysine-ketoglutarate reductase/saccharopine dehydrogenase from developing soybean seeds. Plant Physiol. 123: 655–663.
34. Miron, D., Ben-Yaacov, S., Karchi, H., and Galili, G. 1997. In vitro dephosphorylation inhibits the activity of soybean lysine-ketoglutarate reductase in a lysine-regulated manner. Plant J. 12: 1453–1458.
35. Karchi, H., Shaul, O., and Galili, G. 1994. Lysine synthesis and catabolism are coordinately regulated during tobacco seed development. Proc. Natl. Acad. Sci. USA 91: 2577– 2581.
36. Staswick, P.E. 1994. Storage proteins of vegetative plant tissues. Annu. Rev. Plant Physiol. Mol. Biol. 45: 303–322.
37. Galili, G., Shimoni, Y., Giorini-Silfen, S., Levanony, H., Altschuler, Y., and Shani, N. 1996. Wheat storage proteins: Assembly, transport and deposition in protein bodies. Plant Physiol. Biochem. 34: 245–252.
38. Jiang, L. and Rogers, J.C. 1998. Integral membrane protein sorting to vacuoles in plant cells: evidence for two pathways. J. Cell. Biol. 143: 1183–1199.
39. Galili, G. 1995. Regulation of lysine and threonine synthesis. Plant Cell 7: 899–906.
40. Karchi, H., Shaul, O., and Galili, G. 1993. Seed specific expression of a bacterial desensitized aspartate kinase increases the production of seed threonine and methionine in transgenic tobacco. Plant J. 3: 721–727.
41. Shaul, O. and Galili, G. 1993. Concerted regulation of lysine and threonine synthesis in tobacco plants expressing bacterial feedback-insensitive aspartate kinase and dihydrodipicolinate synthase. Plant Mol. Biol. 23: 759–768.
42. Staehelin, L.A. 1997. The plant ER: A dynamic organelle composed of large number of discrete functional domains. Plant J. 11: 1151–1165.
43. Chrispeels, M.J. 1983. The Golgi apparatus mediates the transport of phytohemagglutinin to the protein body in bean cotyledons. Planta 158: 140–151.
44. Schmid, M., Simpson, D., and Gietl, C. 1999. Programmed cell death in castor bean endosperm is associated with the accumulation and release of a cysteine endopeptidase from ricinosomes. Proc. Natl. Acad. Sci. USA 96: 14159– 14164.
45. Shaul, O. and Galili, G. 1992. Increased lysine synthesis in transgenic tobacco plants expressing a bacterial dihydrodipicolinate synthase in their chloroplasts. Plant J. 2: 203– 209.
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2000-05-13
2018-09-25

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